Polyketides and their synthesis

ABSTRACT

The complete sequence of the gene cluster for the monensin type I polyketide synthase, from  S. cinnamonensis,  is provided. Thus variant polyketides containing monensin-derived elements can be genetically engineered. Furthermore there are novel features, e.g. a regulatory protein mon RI, which are of wide utility.

[0001] The present invention relates to processes and materials (including enzyme systems, nucleic acids, vectors and cultures) for preparing polyketides, particularly polyethers but including polyenes, macrolides and other polyketides by recombinant synthesis, and to the polyketides so produced, particularly novel polyketides. (N.B the term “polyketide” is being used in its conventional sense to include structures notionally derived by the reduction and/or other processing or modification of one or more Ketide units). Furthermore the invention provides the entire nucleic acid sequence of the biosynthetic gene cluster that governs the production of the ionophoric antibiotic polyether polyketide monensin in Streptomyces cinnamonensis, and the use of all or part of the cloned DNA first, in the specific detection of other polyether biosynthetic gene clusters; secondly in the engineering of mutant strains of S. cinnamonensis and of other actinomycetes which are suitable host strains for the high level production of novel recombinant polyketides; and thirdly in the provision of recombinant biosynthetic genes which lead to such novel polyketide products.

[0002] Polyketides are a large and structurally diverse class of natural products that includes many compounds possessing antibiotic or other pharmacological properties, such as erythromycin, tetracyclines, rapamycin, avermectin, monensin, epothilones and FK506. In particular, polyketides are abundantly produced by Streptomyces and related actinomycete bacteria. They are synthesised by the repeated stepwise condensation of acylthioesters in a manner analogous to that of fatty acid biosynthesis. The greater structural diversity found among natural polyketides arises from the selection of (usually) acetate or propionate as “starter” or “extender” units; and from the differing degree of processing of the β-keto group observed after each condensation. Examples of processing steps include reduction to β-hydroxyacyl-, reduction followed by dehydration to 2-enoyl-, and complete reduction to the saturated acylthioester. The stereochemical outcome of these processing steps is also specified for each cycle of chain extension. In addition, the biosynthetic pathways to many polyketides involve additional enzyme-catalysed modifications which may include: methylation by O- and C-methyltransferases, hydroxylation by cytochrome P450 enzymes, other oxidation or reduction processes, and the biosynthesis and attachment of novel sugars and/or deoxy sugars.

[0003] The biosynthesis of polyketides is initiated by a group of chain-forming enzymes known as polyketide synthases. Two classes of polyketide synthase (PKS) have been described in actinomycetes. One class, named Type I PKSs, represented by the PKSs for the macrolides erythromycin, oleandomycin, avermectin and rapamycin, consists of a different set or “module” of enzymes for each cycle of polyketide chain extension. (For examples see Cortés, J. et al. Nature (1990) 348:176-178; Donadio, S. et al. Science (1991) 252:675-679; Swan, D. G. et al. Mol. Gen. Genet. (1994) 242:358-362; MacNeil, D. J. et al. Gene (1992) 115:119-125; Schwecke, T. et al. Proc. Natl. Acad. Sci. USA (1995) 92:7839-7843.)

[0004] The term “extension module” as used herein refers to the set of contiguous domains, from a β-ketoacyl-ACP synthase (“KS”) domain to the next acyl carrier protein (“ACP”) domain, which accomplishes one cycle of polyketide chain extension. The term “loading module” is used to refer to any group of contiguous domains which accomplishes the loading of the starter unit onto the PKS and thus renders it available to the KS domain of the first extension module. The length of polyketide formed has been altered, in the case of erythromycin biosynthesis, by specific relocation using genetic engineering of the enzymatic domain of the erythromycin-producing PKS that contains the chain releasing thioesterase/cyclase activity (Cortés J. et al. Science (1995) 268:1487-1489; Kao, C. M. et al. J. Am. Chem. Soc. (1995) 117:9105-9106).

[0005] In-frame deletion of the DNA encoding part of the ketoreductase domain in module 5 of the erythromycin-producing PKS (also known as 6-deoxyerythronolide B synthase, DEBS) has been shown to lead to the formation of erythromycin analogues 5,6-dideoxy-3-α-mycarosyl-5-oxoerythronolide B, 5,6-dideoxy-5-oxoerythronolide B and 5,6-dideoxy,6-β-epoxy-5-oxoerythronolide B (Donadio, S. et al. Science (1991) 252:675-679). Likewise, alteration of active site residues in the enoylreductase domain of module 4 in DEBS, by genetic engineering of the corresponding PKS-encoding DNA and its introduction into Saccharopolyspora erythraea, led to the production of 6,7-anhydroerythromycin C (Donadio, S. et al. Proc. Natl. Acad. Sci. USA (1993) 90:7119-7123).

[0006] International Patent Application number WO 93/13663 describes additional types of genetic manipulation of the DEBS genes that are capable of producing altered polyketides. However many such attempts are reported to have been unproductive (Hutchinson, C. R. and Fujii, I. Annu. Rev. Microbiol. (1995) 49:201-238, at p. 231). The complete DNA sequence of the genes from Streptomyces hygroscopicus that encode the modular Type I PKS governing the biosynthesis of the macrocyclic immunosuppressant polyketide rapamycin has been disclosed (Schwecke, T. et al. (1995) Proc. Natl. Acad. Sci. USA 92:7839-7843). The DNA sequence is deposited in the EMBL/Genbank Database under the accession number X86780.

[0007] WO 98/01546 discloses that a PKS gene assembly (particularly of Type I) encodes a loading module which is followed by at least one extension module. The first open reading frame encodes the first multi-enzyme or cassette (DEBS1) which consists of three modules: the loading module (ery-load) and two extension modules (modules 1 and 2). The loading module comprises an acyltransferase and an acyl-carrier protein. This may be contrasted with FIG. 1 of WO 93/13663 (referred to above). This shows ORF1 as only two modules, the first of which is in fact both the loading module and the first extension module.

[0008] WO 98/01546 describes in general terms the production of a hybrid PKS gene assembly comprising a loading module and at least one extension module. It also describes (see also Marsden, A. F. A. et al. Science (1998) 279:199-202) construction of a hybrid PKS gene assembly by grafting the wide-specificity loading module for the avermectin-producing polyketide synthase onto the first multi-enzyme component (DEBS1) for the erythromycin PKS in place of the normal loading module. Certain novel polyketides can be prepared using the hybrid PKS gene assembly, as described for example in WO 98/01571.

[0009] WO 98/01546 further describes the construction of a hybrid PKS gene assembly by grafting the loading module for the rapamycin-producing polyketide synthase onto the first multi-enzyme component (DEBS1) for the erythromycin PKS in place of the normal loading module. The loading module of the rapamycin PKS differs from the loading modules of DEBS and the avermectin PKS in that it comprises a CoA ligase domain, an enoylreductase (“ER”) domain and an ACP, so that suitable organic acids including the natural starter unit 3,4-dihydroxycyclohexane carboxylic acid may be activated in situ on the PKS loading domain and, with or without reduction by the ER domain, transferred to the ACP for intramolecular loading of the KS of extension module 1 (Schwecke, T. et al. Proc. Natl. Acad. Sci. USA (1995) 92:7839-7843). WO 98/51695 and WO 98/49315 describe additional types of genetic manipulation of the DEBS genes that are capable of producing altered polyketides.

[0010] The second class of PKS, named Type II PKSs, is represented by the synthases for aromatic compounds. Type II PKSs contain only a single set of enzymatic activities for chain extension and these are re-used as appropriate in successive cycles (Bibb, M. J. et al. EMBO J. (1989) 8:2727-2736; Sherman, D. H. et al. EMBO J. (1989) 8:2717-2725; Fernandez-Moreno, M. A. et al. J. Biol. Chem. (1992) 267:19278-19290). The “extender” units for the Type II PKSs are usually acetate units, and the presence of specific cyclases dictates the preferred pathway for cyclisation of the completed chain into an aromatic product (Hutchinson, C. R. and Fujii, I. Ann. Rev. Microbiol. (1995) 49:201-238). Hybrid polyketides have been obtained by the introduction of cloned Type II PKS gene-containing DNA into another strain containing a different Type II PKS gene cluster, for example by introduction of DNA derived from the gene cluster for actinorhodin, a blue-pigmented polyketide from Streptomyces coelicolor, into an anthraquinone polyketide-producing strain of Streptomyces galileus (Bartel, P. L. et al. J. Bacteriol. (1990) 172:4816-4826).

[0011] The minimal number of domains required for polyketide chain extension on a Type II PKS when expressed in a Streptomyces coelicolor host cell (the “minimal PKS”) has been defined for example in WO 95/08548 as containing the following three polypeptides which are products of the actI genes: firstly KS; secondly a polypeptide termed the CLF with end-to-end amino acid sequence similarity to the KS but in which the essential active site residue of the KS, namely a cysteine residue, is substituted either by a glutamine residue or, in the case of the PKS for a spore pigment such as the whiE gene product (Davis, N. K. and Chater, K. F. Mol. Microbiol. (1990) 4:1679-1691) by a glutamic acid residue; and finally an ACP. The CLF has been stated (for example in WO 95/08548) to be a factor that determines the chain length of the polyketide chain that is produced by the minimal PKS. However it has been found (Shen, B. et al. J. Am. Chem. Soc. (1995) 117:6811-6821) that when the CLF for the octaketide actinorhodin is used to replace the CLF for the decaketide tetracenomycin in host cells of Streptomyces glaucescens, the polyketide product is not found to be altered from a decaketide to an octaketide, so the exact role of the CLF remains unclear. An alternative nomenclature has been proposed in which KS is designated KSα and CLF is designated KSβ, to reflect this lack of knowledge (Meurer, G. et al. Chemistry & Biology (1997) 4:433-443). The mechanism by which acetate starter units and acetate extender units are loaded onto the Type II PKS is not known, but it is speculated that the malonyl-CoA:ACP acyltransferase of the fatty acid synthase of the host cell can fulfil the same function for the Type II PKS (Revill, W. P. et al. J. Bacteriol. (1995) 177:3946-3952).

[0012] WO 95/08548 describes the replacement of actinorhodin PKS genes by heterologous DNA from other Type II PKS gene clusters, to obtain hybrid polyketides. It also describes the construction of a strain of Streptomyces coelicolor which substantially lacks the native gene cluster for actinorhodin, and the use in that strain of a plasmid vector pRM5 derived from the low-copy number vector SCP2* isolated from Streptomyces coelicolor (Bibb, M. J. and Hopwood, D. A. J. Gen. Microbiol. (1981) 126:427-442) and in which heterologous PKS-encoding DNA may be expressed under the control of the divergent actI/actIII promoter region of the actinorhodin gene cluster (Fernandez-Moreno, M. A. et al. J. Biol. Chem. (1992) 267:19278-19290). The plasmid pRM5 also contains DNA from the actinorhodin biosynthetic gene cluster encoding the gene for a specific activator protein, ActII-orf4. The ActII-orf4 protein is required for transcription of the genes placed under the control of the actI/actIII bidirectional promoter and activates gene expression during the transition from growth to stationary phase in the vegetative mycelium (Hallam, S. E. et al. Gene (1988) 74:305-320).

[0013] Type II clusters in Streptomyces are known to be activated by pathway-specific activator genes (Narva, K. E. and Feitelson, J. S. J. Bacteriol. (1990) 172:326-333; Stutzman-Engwall, K. J. et al. J. Bacteriol. (1992) 174:144-154; Fernandez-Moreno, M. A. et al. Cell (1991) 66:769-780; Takano, E. et al. Mol. Microbiol. (1992) 6:2797-2804; Gramajo, H. C. et al. Mol. Microbiol. (1993) 7:837-845). The DnrI gene product complements a mutation in the actII-orf4 gene of S. coelicolor, implying that DnrI and ActII-orf4 proteins act on similar targets. A gene (srmR) has been described (EP 0 524 832 A2) that is located near the Type I PKS gene cluster for the macrolide polyketide spiramycin. This gene specifically activates the production of the macrolide antibiotic spiramycin, but no other examples have been found of such a gene. Also, no homologues of the ActII-orf4/DnrI/RedD family of activators have been described that act on Type I PKS genes. WO 98/01546 describes the use of the ActII-orf4 family of activators in conjunction with their cognate promoters (e.g actII-orf4 with the actI promoter) in a heterologous actinomycete to obtain high level expression of recombinant Type I polyketide synthase genes.

[0014] Although large numbers of therapeutically important polyketides have been identified, there remains a need to obtain novel polyketides that have enhanced properties or possess completely novel bioactivity. The complex polyketides produced by Type I PKSs are particularly valuable, in that they include compounds with known utility as anthelminthics, insecticides, immunosuppressants, antifungal agents or antibacterial agents. Because of their structural complexity, such novel polyketides are not readily obtainable by total chemical synthesis, nor by chemical modifications of known polyketides.

[0015] There is also a need to develop reliable and specific ways of deploying individual genes and portions of genes in practice so that all, or a large fractions of hybrid PKS genes that are constructed, are viable and produce the desired polyketide product. This includes the development of advantageous host strains for expression of such genes. For example many polyketides are rendered bioactive by the action of further enzymes other than the polyketide synthase, and host strains that contain and are able to express the genes for such enzymes are particularly convenient for the efficient synthesis of the bioactive material. In those cases where the construction of a known or a novel polyketide requires specialised precursors, host strains containing and able to express the genes for key enzymes that enhance the production of such specialised precursors are equally valuable and desirable. There is also a need to develop rational methods of increasing the expression level of all the genes required for production of a specific polyketide. Clearly also a host cell which is advantageous for the above reasons, and/or because of other favourable characteristics including but not limited to its speed of growth, excellent handling characteristics in fermentation, and ease of transformation with DNA by various techniques, can be made even more favourable by the cloning into that cell of such auxiliary genes for polyketide modification, or gene activation, or post-translational modification, or precursor supply.

[0016] The DNA sequences have been disclosed for several Type I PKS gene clusters that govern the production of 16-membered macrolide polyketides, including the tylosin PKS from Streptomyces fradiae (application EP 0 791 655 A2), the niddamycin PKS from Streptomyces caelestis (Kavakas, S. J. et al. J. Bacteriol. (1997) 179:7515-7522) and the spiramycin PKS from Streptomyces ambofaciens (application EP 0791 655 A2). DNA sequences have also been disclosed for Type I PKS gene clusters that govern the production of further complex polyketides, for example rifamycin from Amycolatopsis mediterranei (WO 98/07868), and soraphen from Sorangium cellulosum (U.S. Pat. No. 5,716,849), but so far no DNA sequence has been disclosed for one of the most widespread and important classes of complex polyketides, the polyethers.

[0017] Polyethers form an important group of complex polyketide antibiotics (Westley, J. W. in “Antibiotics IV. Biosynthesis” (Corcoran, J. W. Ed.), Springer-Verlag, New York (1981) p. 41-73). They are polyoxygenated carboxylic acids which act as selective ionophores transporting cations across the cell membrane of target cells and thereby causing depolarisation and cell death. Certain polyethers including monensin, lasalocid and tetronasin are in widespread use in animal husbandry as coccidiostats (principally targetted against Eimeria spp.) and as growth promoters. Polyethers have also been reported to be active in vitro and in vivo against the malarial parasite Plasmodium falciparum (Gumila, C. et al. Antimicrobial Agents and Chemotherapy (1997) 41: 523-529).

[0018] Polyethers contain multiple asymmetric centres and are characterised by the presence of tetrahydrofuran and tetrahydropyran rings, producing a characteristic shape which is non-polar on its outer surface and therefore well adapted for transport of material across bacterial membranes; and provides on its inner surface polar coordinating ligands for a centrally-bound metal ion. In addition to tetrahydrofuran and tetrahydropyran rings, other groups which are often present include spiroketal, dispiroketal, and substituted benzoic acid moieties and occasionally other groups for example a tetronic acid or a 6-membered carbocyclic ring

[0019] Monensins A and B are produced by the actinomycete Streptomyces cinnamonensis. Their structures are shown in FIG. 1. Monensin B differs from monensin A only in the presence of a methyl sidechain at C-16 rather than an ethyl sidechain. Monensin selectively binds and transports sodium ions. In addition to its antibacterial and antifungal properties monensin has some activity against protozoal parasites such as the malarial parasite Plasmodium falciparum. Although the structures of polyethers differ significantly from those of other complex polyketides such as the polyhydroxylated and polyene macrolides, their biosynthesis appears to take place by a metabolic pathway which has many common elements. Thus experiments using carbon 14-labelled precursors have shown that monensin A is synthesised from five acetate, one butyrate and seven propionate units (Day, L. E. et al. Antimicrob. Agents Chemother. (1973) 4:410-414). Similarly experiments using precursors doubly-labelled with carbon-13 and oxygen-18 have shown that oxygens (O)1, (O)3, (O)4, (O)5, (O)6 and (O)10 of monensin arise from the carboxylate oxygens of either propionate or acetate, while growth in the presence of oxygen-18 oxygen gas demonstrated that the three remaining ether oxygens (O)7, (O)8 and (O)9 are derived from molecular oxygen (Cane, D. E. et al., J. Am. Chem. Soc. (1981) 103:5962-5965; Cane, D. E. et al. J. Am. Chem. Soc. (1982) 104:7274-7281; Ajaz, A. A. and Robinson, J. A. J. Chem. Soc. Chem. Commun. (1983) 12:679-680). These findings have been rationalised by proposing that the biosynthesis of monensin proceeds via an acyclic triene intermediate (1) in which the geometry of all three carbon-carbon double bonds is E (entgegen) rather than Z (zusammen). The triene is then proposed to be subject to epoxidation to a tri-epoxide (2) and then ring opening is proposed to occur with concomitant sequential formation of the five ether rings as shown in FIG. 2A. Such a biosynthetic pathway, first mooted by Westley in 1974 (Westley J. W. et al., J. Antibiot. (1974) 27:597-604) accounts for the observed stereochemistry at the multiple asymmetric centres in monensin, (Cane, D. E. et al. J. Am. Chem. Soc. (1982) 104:7274-7281; Sood, G. R. et al. J. Chem. Soc. Chem. Commun. (1984) 21:1421-1424) and analogous schemes can be used to account for the biosynthesis of other known polyethers. such as lasalocid A (Hutchinson C. R. et al., J. Am. Chem. Soc. (1981) 103:5953-5956), tetronasin (ICI 139603) (Demetriadou, A. K. et al. J. Chem. Soc. Chem. Commun. (1985) 7:408-410) and narasin (Spavold, Z. et al. Tetrahedron Letters (1986) 27:3299-3302). The hydroxylation at C-26 and the introduction of an O-methyl group on oxygen 3-are proposed to occur as late steps in the biosynthesis, after formation of the polyether structure.

[0020] Unfortunately key aspects of the biosynthetic scheme shown in FIG. 2A have so far eluded experimental confirmation. No biosynthetic intermediates have been isolated from mutants of S. cinnamonensis that are blocked in early stages of monensin production. 26-deoxymonensin A has been isolated from a S. cinnamonensis mutant partially blocked in monensin production (Ashworth, D. M. et al. J. Antibiot. (1989) 42:1088-1099) and 3-0-demethylmonensins A and B have been recovered as minor components from the fermentation broth of a monensin-producing strain (Pospisil, S. et al. J. Antibiot. (1987) 40:555-557). When fed to cells of S. cinnamonensis in radio-labelled form, neither 26-deoxymonensin A, nor 3-0-demethylmonensin A, nor 3-0-demethyl, 26-deoxymonensin A were significantly incorporated into monensin A (Ashworth, D. M. et al. J. Antibiot. (1989) 42:1088-1099), either because they are actively excluded or because these modifications in fact occur earlier in the biosynthetic pathway so that these metabolites are shunt products not readily converted into the final antibiotic by the respective hydroxylase or methyltransferase. Similarly, the putative all (E)-triene precursor (1) has been synthesised and shown not to become incorporated into monensin when fed to growing cells of S. cinnamonensis (Holmes, D. S. et al. Helv. Chim. Acta (1990) 73:239-259). An alternative pathway has been proposed, as shown in FIG. 2B, based on the transition-metal-mediated oxidation of 1,5-dienes (Walba, D. M. and Edwards, P. D. Tetrahedron Lett. (1980) 21:3531-3534). The triene intermediate (4) would different from that of FIG. 2A (1) only in that each carbon-carbon double bond would have the (Z)-configuration (Townsend, C. A. and Basak, A. Tetrahedron (1991) 47:2591-2602) and not the (E)-configuration.

[0021] The genetic basis of secondary metabolite biosynthesis essentially exists in the genes which code for the individual biosynthetic enzymes and in the regulatory elements which control the expression of the biosynthetic genes. The genes encoding biosynthesis of polyketides in actinomycetes have hitherto been found as clusters of adjacent genes, ranging in size from 20 kilobasepairs (kbp) to over 100 kbp. The clusters often contain specific regulatory genes and genes conferring resistance of the producing strain to its own antibiotic.

[0022] In various of its aspects the invention provides the following:

[0023] (1) a DNA sequence encoding at least one-peptide necessary for the biosynthesis of monensin, preferably comprising one or more of the following genes: mon BI, mon BII, mon CI, mon CII, mon H, mon RI, mon RII, mon T, mon AIX and mon AX as depicted in the appended sequence data or an allele or mutation thereof;

[0024] (2) a DNA sequence according to the first aspect comprising all of the genes listed therein or an allele or mutation thereof;

[0025] (3) a DNA sequence according to the first aspect comprising the complete monensin gene cluster;

[0026] (4) a DNA sequence coding for one or more of the peptides set out below, said peptide having the amino acid sequence as set out in the appended sequence data or being a variant thereof having the specified activity: peptide activity mon CII epoxyhydrolase/cyclase mon E S-adenosylmethionine-dependent methyltransferase mon T monensin resistance gene mon RII repressor protein mon AIX thioesterase mon AI polyketide synthase multienzyme mon AII polyketide synthase multienzyme mon AIII polyketide synthase multienzyme mon AIV polyketide synthase multienzyme mon AVI polyketide synthase multienzyme mon AVII polyketide synthase multienzyme mon AVIII polyketide synthase multienzyme mon H regulatory protein mon CI flavin-dependent epoxidase mon BII carbon-carbon double bond isomerase mon BI carbon-carbon double bond isomerase mon D cytochrome P450 hydroxylase mon RI activator protein mon AX thioesterase

[0027] (5) a recombinant cloning or expression vector comprising a DNA sequence according to any of aspects 1-4;

[0028] (6) a transformant host cell which has been transformed to contain a DNA sequence according to any of aspects 1-4 and is capable of expressing a corresponding peptide;

[0029] (7) a hybridization probe comprising a polynucleotide which binds specifically to a region of the monensin gene cluster selected from mon BI, mon BII, mon CI, mon CII, mon H, mon RI, mon RII, mon T, mon AIX and mon AX;

[0030] (8) use of a probe according to aspect (7) in a method of detecting the presence of a gene cluster which governs the synthesis of a polyether, and optionally isolating a gene cluster detected thereby;

[0031] (9) Use of a probe comprising a polynucleotide which binds specifically to a gene responsible for levels of activity of the monensin gene cluster, preferably a regulatory gene, resistance gene or thioesterase gene, more preferably the regulatory gene mon RI, in a method of detecting an analogous gene in a gene cluster of another polyketide, preferably a polyether, and optionally manipulating the gene detected thereby to alter the level of expression of said other polyketide;

[0032] (10) a host cell, preferably Streptomyces cinnamonensis, containing a heterologous gene under the control of the mon RI gene and a monensin promoter;

[0033] (11) use of a portion of the monensin gene cluster having chain terminating activity, preferably comprising at least one of mon AIX and mon AX or a mutant or allele thereof having chain terminating activity, to effect chain release of a peptide other than one required for monensin biosynthesis;

[0034] (12) use of a portion of the monensin gene cluster having carbon-carbon double bond isomerase activity, preferably comprising at least one of mon BI and mon BII or a mutant or allele thereof having isomerase activity to provide a desired stereochemical outcome in the synthesis of a polyketide other than monensin;

[0035] (13) a polypeptide encoded by a portion of the monensin gene cluster, preferably comprising at least one of mon BI and mon BII or a mutant or allele thereof, having carbon-carbon double bond isomerase activity;

[0036] (14) an epoxidase enzyme encoded by mon CI or a derivative or variant thereof having epoxidase activity;

[0037] (15) a cyclase enzyme encoded by mon CII or a derivative or variant thereof having cyclase activity.

[0038] Some embodiments of the invention will now be described by way of example with reference to the accompanying drawings in which:

[0039]FIG. 1 shows the structure of monensins A and B;

[0040]FIG. 2 illustrates proposed biosynthetic pathways;

[0041]FIG. 3 illustrates the proposed organization of the monensin polyketide synthase (PKS) enzyme complex; and

[0042]FIG. 4 illustrates the proposed organization of the monensin biosynthetic gene cluster.

[0043] The overall gene organization of the monensin biosynthetic gene cluster, as shown in FIG. 4, is similar to that previously found for many macrolide biosynthetic gene clusters, which have one or more open reading frames (ORFs) encoding large multifunctional PKSs flanked by other genes which encode functions required for the biosynthesis of the antibiotic. In the case of monensin, there is an unusually high number of distinct ORFs encoding PKS multi-enzymes (eight in total, labelled monAI to monAVIII) but there is again a separate module of enzymes for each cycle of polyketide chain extension, exactly as found for modular PKSs for macrolide biosynthesis (see FIG. 3). Thus there are 12 condensations predicted to be required for the production of the carbon skeleton of monensin, and in agreement with this there are found to be 12 extension modules of PKS enzymes distributed among the 8 PKS ORFs. However, as mentioned in detail below, the other genes in the monensin cluster include genes which have not previously been found in any other gene cluster for the biosynthesis of a complex polyketide, and which are not significantly similar to any genes in published sequence databases. The cloned DNA for these genes is useful to allow the diagnosis that a polyketide biosynthetic gene cluster in any actinomycete, uncovered previously by conventional hybridization against a PKS gene probe from (say) the DEBS or some other characterised PKS gene cluster, is one that governs the synthesis of a polyether; and these genes are also valuable either singly or in combination as specific hybridization probes for the specific detection and isolation of additional polyether biosynthetic gene clusters. Examples of these previously-unknown genes are the genes monBI, monBII, monCI and monCII. In addition the regulatory genes monH monRI, and monRII and the resistance gene monT and the thioesterase genes monAIX and monAX are all useful for the detection of analogous genes in other polyether clusters which are required for the rational manipulation of such genes in order to increase levels of the specific product.

[0044] The cloned and sequenced cluster of genes for monensin biosynthesis is useful secondly in the engineering of mutant strains of S. cinnamonensis and of other actinomycetes which are suitable strains for the high level production of either natural or novel recombinant polyketides. The sequence of the monensin cluster disclosed here shows the surprising fact, that the gene cluster contains a gene monRl whose gene product has an amino acid sequence highly similar to that of actII-orf4, the pathway-specific activator gene which activates the actI and other promoters of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor. The recognition of this aspect of the natural regulation of a Type I PKS cluster is important and valuable because first, it is possible to increase the yield of monensin by increasing the level of the activator MonRI, either by placing the gene monRI under the control of a powerful promoter or arranging for the presence within the cells of one or more additional copies of the monRI gene (as exemplified below); secondly, it will be possible to use the monRI gene as a specific hybridisation probe to locate similar genes in other complex PKS gene clusters, especially other polyether PKS gene clusters but also polyene and macrolide gene clusters and all other Type I modular PKS gene clusters; even in cases where (as for rapamycin and erythromycin) no such gene has been previously found within the currently accepted physical limits of the relevant biosynthetic gene cluster. In such cases the monRI gene probe might be expected to uncover the activator even if it resides on the chromosome at some distance from the main body of the gene cluster; and simple experiments would then show whether the activator(s) so uncovered are involved in regulation of the biosynthesis of those particular metabolites; thirdly, increasing the copy number of the monRI gene or of any of the activator genes uncovered will tend to increase the yield of a heterologous polyketide by “crosstalk” where the activator mimics the presence of the normal activator for the transcription of the genes for that heterologous polyketide synthase. It is clear from recently published work (Wietzorrek, A. and Bibb, M. Mol. Microbiol. (1997) 25:1181-1184) that the ActII-orf4 family of activators exert their effects by binding to promoter regions within the target gene cluster, so it will be possible to use the monRI gene together with monensin promoter regions to drive the high-level transcription and translation of heterologous genes in Streptomyces cinnamonensis, and perhaps in other host strains too; such genes need not be PKS genes or even involved in polyketide biosynthesis. Monensin promoter regions are found at the 5′ end of genes or groups of genes in the cluster and their location is clear from the sequence analysis disclosed here. Thus a useful vector would provide the monensin promoter and the ribosome binding site and continue up to the start of the open reading frame, after which the monensin ORF naturally found there would be replaced by the heterologous gene. The relative strength of the monensin promoters can be readily determined using any one of a number of known promoter probes, i.e. genes whose expression gives rise to readily measurable and quantifiable effects, such as Green Fluorescent Protein (GFP); or beta-galactosidase in the presence of a chromogenic substrate. It should be possible to mutate randomly the small region of the monensin promoters especially likely to interact with the MonRI activator (identified by the presence of tandem heptanucleotide repeats with a common consensus sequence between the various monensin promoters) (Wietzorrek, A. and Bibb, M. Mol. Microbiol. (1997) 25:1181-1184), and to determine the optimal DNA sequence for the maximal activation effect using either S. cinnamonensis (preferably—in case there are other unknown factors that make the activation function better in this strain than in other heterologous systems), or even in another host actinomycete strain. If the natural monensin promoters were mutated to have this optimal recognition sequence, then this would further increase the production of monensin. By extension, the use of this modified monensin promoter in conjunction with the monRI gene in heterologous systems could form the basis of further improvements in expression of polyketide synthases or other genes, either by appropriate chromosomal alterations to introduce the altered promoter and also the monRI gene; or by provision of vectors containing these optimised signals linked to specific genes and housed in suitable host cells.

[0045] The sequencing of the monensin cluster has uncovered another strategy for gene regulation in such Type I clusters. The previously-sequenced genes for the rapamycin biosynthetic pathway in Streptomyces hygroscopicus included a gene of unknown function (rapH). A closely similar gene has now been found in the monensin biosynthetic gene cluster (monH), and it is clear from this recurrence (and the comparison of the sequences with those of database proteins) that this gene is potentially an important DNA-binding sensor gene which acts to regulate the transcription of the cluster in concert with other regulatory signals. Simple experimentation is needed in order to define whether the gene is an activator, in which case putting in another copy or increasing its transcription will have the potential to increase polyketide biosynthesis; or alternatively the rapH gene product may be a negative regulator, whereupon deletion of this gene may release the biosynthetic pathway from this inhibitory effect and increase yields.

[0046] There is a continuing need to develop new methods of high-level production of bioactive metabolites and other valuable gene products in actinomycetes. Streptomyces cinnamonensis is a recognised and very valuable industrial strain for the production of very high levels of monensin, it is readily transformable with DNA by standard methods of conjugation or of protoplast transformation, it is a host for numerous known broad range plasmids including well-known expression plasmids of both high- and low-copy number, it also grows quickly relative to other actinomycete strains (for example about three times faster than wild type Saccharopolyspora erythraea the erythromycin producer, under comparable conditions) and sporulates relatively easily. Heterologous polyketides can be expressed in Streptomyces cinnamonensis using for example the low-copy number plasmid pCJR24 (which has no origin of replication active in actinomycetes so is maintained by integration into the chromosome) (Rowe, C. et al. Gene (1998) 216:215-223) or the related plasmid pCJR29 in which the polyketide synthase gene(s) are placed under the control of the acti promoter which is activated by the ActII-orf4 activator; or alternatively the monAI promoter can be substituted together with the MonRI activator; or some other pairing of activator and cognate promoter chosen from either a Type II or a Type I polyketide synthase gene cluster. As an example, the wild type strain of Streptomyces cinnamonensis has been used to express the plasmid pCJR29 (Rowe, C. et al. Gene (1998) 216:215-223) containing as insert the three ORFs for the PKS governing the production of 6-deoxyerythronolide B, the macrolide precursor of erythromycin A in Saccharopolyspora erythraea, these genes being placed under the control of the pathway-specific actI promoter from Streptomyces coelicolor together with its cognate activator gene actII-orf4. The transformed strain when cultivated in a suitable liquid medium produced 6-deoxyerythronolide B in good yield.

[0047] It is well known to the person skilled in the art that it is possible to use standard vectors unable to replicate in actinomycetes to introduce DNA into a Streptomyces cell, such DNA comprising two portions of contiguous DNA which are each identical to one of two portions of the cell's chromosome that are spaced up to 100 kbp apart; and that through recombination between the incoming DNA and the chromosome occurring in both portions of DNA the net result is that the chromosomal sequence is replaced by the defective sequence originally that of the incoming DNA. Such a procedure has been applied to the monensin-producing strain of S. cinnamonensis as described in detail below, and a strain of S. cinnamonensis has been obtained that carries a specific deletion in the monensin cluster and which is unable to produce the antibiotic. The use of such a strain facilitates the production of heterologous polyketides by removal of the background of monensin production.

[0048] The multiple uses of portions of the cloned and sequenced DNA from the monensin cluster will readily occur to the person skilled in the art. A surprising feature of the PKS of the monensin cluster is an unusual mechanism of polyketide chain initiation. We have found that the monensin PKS loading module has three domains, which from the amino-terminus of the protein are: a KSq domain, an acyltransferase domain and an ACP domain. We have uncovered this organisation in the PKS for the 14-membered macrolide oleandomycin as well as in the monensin PKS, an organisation of the loading module previously only found for the 16-membered macrolides and in which the KSq domain (which looks like a ketosynthase or condensation domain except that the active site cysteine residue is substituted by a glutamine for which the single letter notation is Q) had been previously speculated to have no function. It was realised that the acyltransferase of the loading module actually has malonyl-CoA and not acetyl-CoA as a substrate and that KSq is an active decarboxylase. It appears that a better discrimination can be achieved in the selection of the smaller acetate unit over propionate if the choice is made initially between methylmalonyl- and malonyl-CoA.

[0049] An unprecedented feature of the monensin PKS genes is that no integral chain-terminating domain is present as a C-terminal appendage of the PKS extension module that catalyzes the twelfth and final chain extension. Because the product of the monensin PKS is a carboxylic acid, it would have been firmly predicted that chain release would have been catalyzed by such a C-terminal domain containing a “thioesterase” activity. Previously sequenced PKS gene sets have been of two sorts: first, those macrolide PKSs typified by erythromycin, spiramycin, tylosin, niddamycin which have a readily recognisable C-terminal “thioesterase” domain, which in these enzymes functions as a specific cyclase rather than releasing the polyketide product as a free carboxylic acid; secondly, those macrolide PKSs typified by rapamycin, FK506, and rifamycin, where there is an alternative and recognised mode of chain termination by transfer of the polyketide chain to an acceptor moiety, catalyzed by a specific enzyme (eg pipecolate incorporating enzyme for rapamycin (Schwecke T. et al. Proc. Natl. Acad. Sci. USA (1995) 92:7839-7843) and FK506 (Mothamedi H. and Shafiee A, Eur. J. Biochemistry (1998) 256:528-534); arylamine synthetase for rifamycin (August P. R. et al. Chemistry & Biology (1998) 5:69-79).

[0050] The monensin PKS surprisingly falls into neither category, and therefore seems to be the first example of a novel mode of chain termination. It is novel and noteworthy in this connection that the monensin PKS gene cluster contains two small genes that encode discrete, monofunctional thioesterase enzymes. Although many PKS gene clusters have been previously shown to contain one such discrete thioesterase, none have been shown to have two. The role of such thioesterases is not known, although in the case of methymycin/pikromycin PKS, which has been reported to be responsible for the biosynthesis of both the 12-membered macrolide methymycin and the 14-membered macrolide pikromycin (Xue Y. Q. Proc. Natl. Acad. Sci. USA (1998) 95:12111-12116) the disruption of this thioesterase reportedly caused a ten-fold drop in the amount of both macrolides produced. A similar finding has been reported for the discrete thioesterase of the tylosin PKS gene cluster (Cundliffe E. et al. Chemistry & Biology in press). Additional copies of such thioesterases may therefore accelerate the production of specific polyketide, but this has not yet been demonstrated. However, the presence of the discrete thioesterase is not completely essential for polyketide production.

[0051] It is highly desirable to have a broadly effective method of catalysing the release of polyketide gene products from a PKS as the free acid. The well-studied integral thioesterase domain in the erythromycin PKS thioesterase has a broad specificity in cyclization to form a lactone (assuming that a hydroxy group is present in the growing polyketide chain at an appropriate position), but hydrolysis to form the free acid is very slow. The recognition of the unusual arrangement of the monensin PKS means that it is now possible to harness either the entire PKS module that catalyses the twelfth and final extension cycle in monensin biosynthesis, or the C-terminal portion of it, and graft it onto a different polyketide synthase by genetic engineering, so as to allow the release mechanism characteristic of monensin to operate in a different context. The use of this portion only of the monensin PKS suffices to allow the novel mechanism of chain release to operate successfully. The speed of the polyketide chain hydrolysis in a given case can depend on the additional presence of one or both of the discrete thioesterase genes (monAIX and monAX) from the monensin gene cluster. The use of this novel method of chain termination represents a valuable way of generating a large number of novel engineered polyketides that are currently inaccessible, and ensuring that the products have a specified chain length.

[0052] The genes monBI and monBII appear to encode very similar enzymes with significant amino acid sequence similarity to authentic ketosteroid isomerases which are known to catalyse the migration of an activated carbon-carbon double bond. The conservation of active site residues makes it very likely that these mon genes govern a reaction involving activated double bonds in the biosynthetic pathway to monensin and this surprising observation can be accommodated if the initial product of the polyketide chain growth on the monensin PKS is a linear precursor in which the double bonds were initially formed with a conventional trans or E (entgegen) geometry; but before the polyketide chain was extended by insertion of the next unit the monBI and/or the monBII gene product(s) catalyse the specific rearrangement of the newly-created double bond into the cis or Z (zusammen) geometry. This new view of the monensin biosynthetic pathway allows the deduction that the monBI and monBII genes, perhaps in combination with specific portions of the monensin modules where they normally exert their effects (namely modules 3, 5 and 7) might be used in order to achieve the extremely desirable targetted biosynthesis of novel polyketides containing double bonds with Z geometry at specified point(s) along the chain. Thus for example it should be possible to provide for the direct biosynthesis of C22-C23 cis or Z double bond in avermectins, thus avoiding tedious and expensive chemical conversion of an initial fermentation product into this important anthelminthic. Only limited experimentation is needed to see whether the monBI and/or monBII gene products are sufficient or whether the mon PKS at modules 3, 5 and 7 forms part of the specific docking site(s) for the isomerases and therefore must also be used in the creation of the hybrid PKS that will insert the cis or Z double bond at the desired position. The substrate specificity of the isomerases need not be limited to 2,3-unsaturated thioesters. The purified enzymes could also be used to effect such isomerisations in vitro, depending on the position of the equilibrium or whether further enzymes are used to achieve the further transformation of the product as it is formed (vide infra).

[0053] The product of the monCI gene is a novel oxidative enzyme with some sequence similarity to authentic examples of such enzymes in the databases; and with a clearly definable role in the monensin biosynthetic pathway, the epoxidation of the double bonds at three separate positions in the initially-formed acyclic intermediate in monensin biosynthesis. This epoxidase could therefore be used in conjunction with monBI/monBII gene products to effect oxidative reactions on suitable substrates in vitro and in vivo. Similarly the monCII gene product is a putative cyclase that opens the epoxides and causes the formation of ether rings in monensin.

[0054] Any or all of the monBI, monBII, monCI or monCII genes may be introduced into a heterologous strain containing the gene cluster for another polyether, in order to divert the biosynthetic pathway and produce a polyketide of altered structure. In these experiments the analogues of these monB genes could either be present or (once located and characterised using the mon genes as probes) they may be deleted prior to the introduction of the monB and monC genes into that strain. The converse experiment in which analogues of the monB and monC genes from other strains are introduced into S. cinnamonensis likewise has the potential to produce novel oxidised polyketides. Also, the monB and monC genes or their analogues may be introduced into a strain that normally produces a macrolide or a polyene or some other complex polyketide and expressed there, when they may effect the diversion of the growing polyketide chain on a heterologous modular PKS towards a new product, which may or may not have the structure of a polyether.

[0055] The availability of the monensin gene sequence allows the institution of domain swaps to alter the acyltransferase (AT) specificity of a given module, for example the ethylmalonyl-CoA specific extender found in one of the modules of the monensin PKS can be used to replace one of the other ATs to generate an ethyl side branch at that position in the chain, or the AT can be used to substitute in any other (e.g. macrolide) PKS, as described in WO 98/01571 and Wo 98/01546. Similarly the alteration of the level of reduction in a module, by manipulation of the reductive enzymes, can be applied to the monensin genes and here it will produce, depending on which module is affected, either an altered monensin, or a species which is only partly cyclised, or a polyether with an altered pattern of cyclisation, or even a linear polyketide.

[0056] In general the targetted alteration of the pattern of substitution of sidechains or reduction level along the polyketide chain produced by the monensin PKS will, like the disruption or deletion of the oxidative enzymes mentioned above, lead to non-polyether polyketide products. It should be possible, by introduction of the DEBS thioesterase at the C-terminus of one of the later modules of the monensin PKS, together with an appropriately placed hydroxy group earlier in the chain, to produce novel macrolide products from this polyether PKS system, or alternatively novel polyenes of defined chain length and chosen ring size.

EXAMPLE 1 Cloning of the Monensin A Biosynthetic Gene Cluster Using DNA Probes Derived From the Erythromycin-Producing Polyketide Synthase of Saccharopolyspora erythraea

[0057] A genomic library of the monensin A producing strain Streptomyces cinnamonensis ATCC 15413 was constructed using methods well-known in the art, namely, the production of high molecular weight genomic DNA, followed by the partial cleavage of this DNA using the frequent-cutting restriction enzyme Sau3A, fractionation of the fragments on a sucrose gradient and selection of fragments of average size 35-40 kbp, and the cloning of these fragments into the cosmid vector pWE15 (Evans, G. A. et al. Gene (1989) 79:9-20) which had been previously digested with BamHI and treated with shrimp alkaline phosphatase. The library was packaged and transfected into Escherichia coli XL-1 Blue MR cells. The library was plated out on 2×TY agar medium (10 g tryptone, 10 g yeast extract, 5 g NaCl, 15 g bactoagar per litre containing ampicillin 50 μg/ml) for cosmid selection and the colonies were allowed to grow overnight. The library was then screened by hybridisation using as a probe DNA encoding the ketosynthase domain of module 1 of the erythromycin-producing PKS (6-deoxyerythronolide B synthase, DEBS) of Saccharopolyspora erythraea. The colonies giving a positive hybridisation signal in the hybridisation were selected and the cosmid DNA from each colony was purified and mapped by restriction digestion. The presence of the target biosynthetic genes on a cosmid was verified by sequencing of the ends of the cosmid inserts using the commercially available T3 and T7 primers which hybridise specifically to the respective ends of each cosmid insert (Evans, G. A. et al. Gene (1989) 79:9-20).

EXAMPLE 2 Sequencing of the Biosynthetic Gene Cluster for Monensin A From Streptomyces cinnamonensis

[0058] Three cosmids obtained by screening of the genomic library of S. cinnamonensis were used to obtain the entire DNA sequence of the monensin biosynthetic gene cluster. These cosmids, MO.CN02, MO.CN11 and MO.CN33 between them contain the entire DNA sequence of the cluster and the adjacent regions of the chromosome. They have been deposited in NCIMB, 23 St Machair Drive, Aberdeen AB24 3RY, UK, under the NCIMB accession numbers 40956 (MO-CN11); 40957 (MO-CN33) and 40958 (MO-CN02) respectively.

[0059] The DNA of each cosmid was separately subjected to partial digestion with Sau3A and fragments of approximately 1.5-2.0 kbp were separated by agarose gel electrophoresis. The fragments were then ligated into the plasmid vector pUC18 (Messing, 1982), previously digested with BamHI and treated with shrimp alkaline phosphatase. The library was transformed into E. Coli strain XL1-Blue MR and plated on 2×TY agar medium containing ampicillin (100 μg/ml) to select for plasmid-containing cells. Plasmid DNA was purified from individual colonies and sequenced using the Sanger dye-terminator procedure on an ABI 377 automated sequencer (Sanger, F. Science (1981) 214:1205-1210). The sequence data obtained from single random subclones of a cosmid was assembled into a single continuous sequence and edited using GAP4.1 program of the STADEN gene analysis package (Staden, R. Molecular Biotechnology (1996) 5:233-241).

[0060] The sequence is set out in the appended sequence listing.

[0061] Tables I and II contain data about individual genes and gene products.

EXAMPLE 3 Inactivation of the Monensin A Biosynthetic Gene Cluster

[0062] A chromosomal gene disruption experiment was used to verify the identity of the cloned polyketide synthase gene cluster. Plasmid pMOB6314 is a pUC18 sequencing subclone of the presumed monensin A biosynthetic gene cluster prepared as described in Example 1, whose inserted DNA comprises the DNA sequence from nucleotide 9763 to nucleotide 10108 in SEQ ID 1, and which therefore contains a region of DNA wholly internal to orfE, a putative 3-O-methyltransferase. A HindIII fragment containing the thiostrepton resistance gene tsr from plasmid pIJ702 (Katz, E. et al. J. Gen. Microbiol. (1983) 129:2703-2714) was cloned into the HindIII site of plasmid pMOB6314 and the ligation mixture was used to transform E. coli cells. Transformants bearing the required plasmid pMOΔE01 were identified by isolation of plasmid DNA and analysis by restriction digestion. pMOΔE01. Plasmid pMOΔE01 was used to transform protoplasts of Streptomyces cinnamonensis as described by (Hopwood D. A. et al. (1985)). Since plasmid pMOΔE01 lacks an origin of replication that is active in Streptomyces, growth in the presence of thiostrepton (25 μg/ml) in the regeneration medium led to the isolation of stable integrants. Isolated putative integrants were tested for the presence of integrated pMOΔE01 sequences by Southern hybridisation. A clone of Streptomyces cinnamonensis identified by its restriction pattern in Southern hybridisation as bearing pMOΔE01 integrated in the region of monE of the monensin A biosynthetic gene cluster was designated S. cinnamonensis MO-DD01.

[0063] Detection of production of the monensin A related metabolites produced by S. cinnamonensis MO-DD01 was performed by GC-MS analysis of methanol extracts of the entire broth harvested in 72 hours of growth of the strain. No significant amounts of monensin A-related metabolite production were detectable.

EXAMPLE 4 Overproduction of Erythromycin Aglycone in Streptomyces cinnamonensis

[0064]S. cinnamonensis is a suitable system for overproduction not just of monensin A but also of other polyketide metabolites. Established techniques of genetic transformation allow fast introduction of foreign polyketide producing genes sets into this host. Fast growth of S. cinnamonensis in liquid culture and optimal precursor supply favour high yield of polyketide metabolites.

[0065] Construction of pIB061

[0066]S. erythraea NRRL2338 was transformed with pCJR30 (Rowe, C. J., et al. (1998) Gene 216:215-223) using a routine protoplast transformation technique as described by Hopwood et al. (1985). A stable integrant of S. erythraea [pCJR30] was identified and the production of 10 mg/L of the triketide lactone (delta lactone of (2S,3R,4R,5R)-2,4-dimethyl-3,5-dihydroxy-heptanoic acid) in addition to erythromycins was confirmed by MS analysis.

[0067] Total DNA of S. erythraea [pCJR30] was purified and approximately 200 ng was digested with EcoRI endonuclease. The digestion mixture was precipitated with isopropanol and the resulting DNA was treated with T4 DNA-ligase for 16 hours at 16° C. The ligation mixture was used to transform E.coli DH10B cells. The transformants were screened for the presence of the plasmid. A clone containing a 44.7kb plasmid was identified and confirmed by restriction analysis to contain three complete genes: eryAI, eryAII and eryAIII. The plasmid was named pIB061.

[0068] Transformation of S. cinnamonensis

[0069] Protoplasts of S. cinnamonensis were prepared by a modified procedure of Hopwood et al. (1985). Plasmid pIB061 was transformed into the protoplasts of S. cinnamonensis and stable thiostrepton resistant colonies were isolated. Individual colonies were checked for their plasmid content and the presence of plasmid pIB061 was confirmed by its restriction pattern. S. cinnamonensis (pIB061) was inoculated into 250 ml of M-C3 minimal production medium containing 10 μg/ml of thiostrepton and allowed to grow for 72 hours at 30° C. After this time the mycelia were removed by filtering. The broth was extracted with two volumes of ethyl acetate and the combined ethyl acetate extracts were washed with an equal volume of saturated sodium chloride, dried over anhydrous sodium sulphate, and the ethyl acetate was removed under reduced pressure to give about 200 mg of crude product. The product was analysed by LCQ and mass was confirmed to that of erythronolide B.

[0070] This example demonstrates the importance of S. cinnamonensis for production of high levels of foreign polyketide antibiotics. Introduction of the complete erythromycin gene cluster or other gene clusters into this system are likely to produce high levels of the corresponding metabolites.

EXAMPLE 5 Construction of Plasmid pCJW58 Containing the Monensin Activator Gene Under the ermE* Promoter

[0071] The ermE* promoter derived from the ermE resistance methyltransferase gene of S. erythraea (Bibb et al. Gene (1985) 38:215-226) was amplified by PCR as a SpeI-XbaI fragment using the following oligonucleotides 5′-CCACTAGTATGCATGCGAGTGTCCGTTCGAGT-3′ and 5′-TTGTATACACCTAGGATGGTTGGCCGTGC-3′ with pRH3 (Dhillon et al. Molecular Microbiology (1989) 3:1405-1414 as a template and cloned into SmaI-digested, phosphatase-treated pUC18, to produce plasmid pIB135. The integrative plasmid pSET152 (Bierman, M. et al. (1992) Gene 116:43-49)) was digested with XbaI and the backbone was dephosphorylated and ligated to the SpeI-XbaI fragment of pIB135 containing the ermE* promoter. The ligation mixture was used to transform E. coli DH10B and the orientation of the insert in the plasmids from individual clones was checked by using restriction analysis. A plasmid with the ermE* promoter oriented so that the NdeI and XbaI sites are adjacent to the apramycin resistance gene was selected and named pIB139.

[0072] The monR gene from the monensin biosynthetic gene cluster was amplified and NdeI and XbaI restriction sites introduced at 5′ and 3′ ends respectively, by PCR using as primers the following oligonucleotides: 5′-AGA TAC CAT ATG CTG GGC CCG CTC CGC AT-3′ and 5′-AAT GCT CTA GAC TGT CAG CGA CCG GAC AGG GCC AA-3′ and cosmid MO.CN11 as template. The PCR product was ligated into SmaI-treated and phosphatase-treated plasmid pUC18 and the ligation mixture was used to transform E. coli DH10B cells. Transformant colonies were analysed for the presence of plasmid and the identity of the plasmid inserts was verified by sequencing. A plasmid whose insert contained the monR gene flanked by NdeI and XbaI restriction sites was selected and designated pCJW57.

[0073] Plasmid pCJW57 was digested with NdeI and XbaI and the fragment containing the monR gene was ligated together with the backbone of plasmid pIB139 which had been digested with the same two restriction enzymes, and purified by gel elution. The ligation mixture was used to transform E. coli strain DH10B cells. Transformant colonies were analysed for the presence of plasmid and the identity of the plasmid inserts was verified by restriction analysis. One such recombinant was selected and named plasmid pCJW58.

[0074] Plasmid pCJW58 was used to transform the methylation-deficient E. coli strain ET 12567 (MacNeil D. J. et al. (1992) Gene 111:61-68) and the recovered, unmethylated plasmid was then used to transform the same E. coli strain ET12567 housing the plasmid pUB307, a derivative of RP4 which is mob and which contains a gene for kanamycin resistance (Piffaretti, J. C. et al. (1988) Mol. Gen. Genet. 212:215-218). Recombinants were plated on 2×TY agar medium containing apramycin and kanamycin at final concentrations of 50 micrograms per ml and 50 micrograms per ml respectively. The plasmid content of recombinants was checked isolation of plasmid DNA and checking of the identity of these plasmids by restriction analysis. One such clone which contained both pUB307 and plasmid pCJW58 was selected and used for further experiments.

[0075] Construction of Streptomyces cinnamonensis (pCJW58) and production of monensins

[0076] A single colony of E. coli ET12567 housing both pUB307 and pCJW58 was toothpicked into 3 ml of TY liquid medium, containing apramycin and kanamycin at 25 and 25 micrograms respectively, and grown overnight at 37° C. This culture was used to inoculate 25 ml of TY medium, supplemented with the same antibiotics at the same concentrations, and growth was continued until the absorbance at 600 nm (1 cm pathlength) was between 0.3-0.6. The cells were centrifuged (room temperature, 7 minutes, 2000×g), resuspended in TY liquid medium (10 ml) containing no added antibiotics, re-centrifuged as before, then resuspended in 2 ml of TSB medium and placed on ice. Meanwhile, 0.5 ml of TSB medium was added to 100 microL containing approximately 10⁸ spores of S. cinnamonensis. After a brief heat shock, at 50° C. for 10 minutes, the suspension was briefly cooled, mixed with 0.5 ml of donor E. coli cells, and plated on solid A medium, which has composition as follows: A medium Sigma wheat starch   5 g Corn steep powder 1.25 g Yeast extract  1.5 g CaCO₃  1.5 g FeSO₄   6 mg DIFCO agar   10 g H₂O to 500 ml

[0077] And to which in addition was added 10 mM MgCl₂ to a final concentration of 10 mM.

[0078] The plates were allowed to dry overnight at room temperature, and were then allowed to incubate a further 18 hours at 30° C. After this time each 25 ml plate was overlaid with a solution of apramycin (final concentration 50 micrograms per ml) and nalidixic acid (final concentration 20 micrograms per ml), and the plates were allowed to incubate for four days at 30° C. At this time individual colonies were toothpicked onto solid A medium and allowed to grow. Four representative colonies from the A medium plate were grown up in liquid modified YEME medium, which has composition as follows: Modified YEME medium Sucrose 100 g DIFCO Yeast extract  3 g Bacto peptone  5 g Oxoid Malt extract  3 g Glucose  10 g H₂O to 1 L

[0079] These cultures were used to provide a 2% vol/vol inoculum for 30 ml of modified YEME which was grown for 7 days, and then transferred to SM16 medium, which has composition as follows: SM16 medium 3-[N-Morpholino]-propane sulfonic acid  20.9 g (MOPS) buffer L-proline  10.0 g Glucose   20 g NaCl  0.5 g K₂HPO₄  2.1 g Ethylenediaminetetraacetic acid, sodium  0.25 g salt MgSO₄.7H₂O  0.49 g CaCl₂.2H₂O 0.029 g Trace elements solution (Hopwood, D. A.    2 ml et al. (1985) Genetic Manipulation of Streptomyces - a Laboratory Manual, at p.235) 0.5 M CoCl₂ solution    2 microliters H₂0 to 1 L

[0080] After growth for a further 7 days, mycelium was collected by centrifugation at 2000×g for 30 minutes, and the supernatant was extracted three times with 300 ml of ethyl acetate. The combined extracts were concentrated by evaporation under reduced pressure to an oil, which was mixed with 1 ml of methanol. Samples were applied to an LCQ liquid chromatograph fitted with a mass spectrometer detector unit. The column used was a C18 reversed phase column, equilibrated with a mixture of 80% 20 mM ammonium acetate/20% acetonitrile, and the column was eluted with a gradient of increasing acetonitrile, reaching 100% acetonitrile over 24 minutes. Monensins A and B emerged from the column with retention times respectively of 8.2 minutes and 9.2 minutes. The relative amounts of monensin produced by three independent clones (A-C) containing an additional copy of the monr gene were compared to a control fermentation of the wild type S. cinnamonensis strain, with the results shown in the Table below: Table showing increased monensin production in strains bearing additional copy of monR gene monensin A monensin B concentration concentration Strain (arbitrary units) (arbitrary units) Control 188  861 A 430 1 800 B 450 1 300 C 249 1 300

EXAMPLE 6 Construction of S. cinnamonensis M12AT5

[0081] A region lying immediately 5′ of the DNA encoding the acyltransferase (AT12) domain of module 12 of the monensin polyketide synthase in the mbnensin biosynthetic gene cluster was amplified with the following primers: 5′-GGTGGCCACGGAAACACCAACACCGGACCCGCGCC-3′, and 5′-CTCTCGGAGGCCCGGCGCAACGGCCACAA-3′, 3′ using casmid MO-CN11 as a template. The PCR product was ligated into SmaI digested and phosphatase-treated plasmid pUC18 and the ligation mixture was used to transform E. coli DH10B cells. Transformant colonies were analysed for the presence of plasmid and the identity of the plasmid inserts was verified by sequencing. A plasmid whose insert contained a fragment upstream of the AT12-encoding sequence from about 82.3kb to 83.2kb of the mon cluster was designated pMO81. Similarly a region lying immediately 3′ of the DNA encoding the acyltransferase (AT12) domain of module 12 of the monensin polyketide synthase in the monensin biosynthetic gene cluster was amplified with the following primers: 5′-GGCCTAGGGCTGCCTCGGGTGGTGGATCTGCCGA-3′ and 5′- TGGTCGGGCGCGGTGCGTGCGATACGT-3′, using cosmid MO-CN11 as a template. The PCR product was ligated into SmaI-treated and dephosphorylated pUC18 and the ligation mixture was used to transform DH10B E.coli cells. Transformant colonies were analysed for the presence of plasmid and the identity of the plasmid inserts was verified by sequencing. A plasmid whose insert contained a fragment downstream of the AT12-encoding sequence, from 80.5kb to 81.4kb of the mon cluster, was designated pMO82.

[0082] The DNA encoding AT of module 5 was amplified and MscI and AvrII restriction enzyme recognition sites were introduced at the ends by PCR using the following primers: 5′-CCTGGCCAGGGCGGCCAGTGGGTGGGCATG-3′ and 5′-GGCCTAGGGGTCGGCCGGGAACCAGCGCCGCCAGT-3′ and the cosmid MO-CN33 as a template. The PCR product was ligated into SmaI-treated and dephosphorylated pUC18 and the ligation mixture was used to transform DH10B E.coli cells. Transformant colonies were analysed for the presence of plasmid and the identity of the plasmid inserts was verified by sequencing. A plasmid whose insert DNA, with sequence from about 44.2kb to 45.2kb of the mon cluster, encoded the AT5 domain was designated pMO83.

[0083] pMO81 was digested with MscI and HindIII and ligated to the 0.9kb MscI-HindIII fragment of pMO82. A clone containing both fragments was designated pMO84. Plasmid pMO84 was cleaved with AvrII and HindIII, treated with phosphatase, and ligated together with the 1.0 kb AvrII-HindIII fragment of pMO83 to produce pMO85, which contains the DNA encoding the AT5 domain flanked by DNA from either side of the DNA encoding the AT12 domain of the monensin PKS. The thiostrepton resistance gene tsr, derived from plasmid pIJ702 (Katz, E. et al., J. Gen. Microbiol. 1983), was cloned into the HindIII site of pMO85. The resulting plasmid pMO86 was analysed by its restriction pattern and confirmed to contain all the desired elements.

[0084] Plasmid pMO86 was used to transform S. cinnamonensis protoplasts as described by Hopwood, D. A. (1985). Stable thiostrepton-resistant transformants were isolated and checked for the desired integration of the pMO85 into the AT12 flanking regions by Southern blot hybridisation. One such integrant, S. cinnamonensis MO-08, containing pMO85 integrated upstream of the AT12, was passed through 4 cycles of sporulation on a non-selective nutrient medium. Spores obtained after the fourth cycle were replica-plated onto media with and without thiostrepton. DNA of clones that had lost thiostrepton resistance was analysed by Southern blot hybridisation. Clones in which the DNA encoding the AT12 domain had been replace by the DNA encoding the AT5 domain was designated S. cinnamonensis M12-AT5. At this time individual colonies were toothpicked onto solid A medium and allowed to grow. Four representative colonies from the A medium plate were grown up in liquid modified YEME medium, which has composition as follows: Modified YEME medium Sucrose 100 g DIFCO Yeast extract  3 g Bacto peptone  5 g Oxoid Malt extract  3 g Glucose  10 g H₂O to 1 L

[0085] These cultures were used to provide a 2% vol/vol inoculum for 30 ml of modified YEME which was grown for 7 days, and then transferred to SM16 medium, which has composition as follows: SM16 medium 3-[N-Morpholino]-propane sulfonic  20.9 g acid (MOPS) buffer L-proline  10.0 g Glucose   20 g NaCl  0.5 g K₂HPO₄  2.1 g Ethylenediaminetetraacetic acid,  0.25 g sodium salt MgSO₄.7H₂O  0.49 g CaCl₂.2H₂O 0.029 g Trace elements solution (Hopwood, D. A.    2 ml et al. (1985) Genetic Manipulation of Streptomyces - a Laboratory Manual, at p. 235) 0.5 M CoCl₂ solution    2 microliters H₂0 to 1 L

[0086] After growth for a further 7 days, mycelium was collected by centrifugation at 2000×g for 30 minutes, and the supernatant was extracted three times with 300 ml of ethyl acetate. To confirm presence of the C-2-ethyl substituents of both monensin A and B the combined extracts were concentrated by evaporation under reduced pressure to an oil, which was mixed with 1 ml of methanol. Samples were applied to an LCQ liquid chromatograph fitted with a mass spectrometer detector unit. The column used was a C18 reversed phase column, equilibrated with a mixture of 80% 20 mM ammonium acetate/20% acetonitrile, and the column was eluted with a gradient of increasing acetonitrile, reaching 100% acetonitrile over 24 minutes. Mass ions 14 mass units above those expected for both monensin A and B confirmed production of the respective C-2-ethyl substituents.

EXAMPLE 7 Construction of pSGK005 and Its Use in the Production of C-13 Propyl-Erythromycin

[0087] Plasmid pSGK005 is a pCJR24 based plasmid containing a PKS gene comprising a loading module plus the first and second extension modules and the chain terminating thioesterase of the PKS responsible for the production of erythromycin (DEBS). The loading module comprises the KS and ethyl-malonyl CoA specific AT from module 5 of the monensin PKS linked to the DEBS loading ACP domain. In addition, the active site cysteine of this module 5 KS has been mutated to glutamine to convert an extender di-domain to a loading di-domain. Plasmid pSGK005 was constructed as follows.

[0088] A 2769 bp DNA segment of the monensin cluster of S. cinnamonensis extending from nucleotide 42438 to 45207 was amplified by PCR using the following oligonucleotide primers. 5′-GTGACGTCATATGTCGAGTGCTGAAGAGTCG-3′ and 5′-GGGGTCGCCTAGGAACCAGCGCCGCCAGTCGA-3′

[0089] The design of these primers introduced Nde I and Avr II sites at the ends of the amplifed fragment. Monensin cosmid 05 was used as a template for the reaction. The resulting 2769 bp fragment was digested with Nde I and Xho I and a 656 bp fragment (Fragment A) purified by preparative gel electrophoresis.

[0090] A second PCR reaction was used with the same template to amplify DNA from nucleotide 43098 to 45207. The primers used were 5′-CGGCCTCGAGGGCCCGTCGGTCAGTGTCGACACGGCGCAGTCCTCCT CGC-3′ and 5′-GGGGTCGCCTAGGAACCAGCGCCGCCAGTCGA-3′

[0091] The design of the upstream oligonucleotide primer incorporated a change of the codon specifying the KS active site cysteine (nucleotides 43135-43137, TGC) to glutamine (CAG). The resulting 2109 bp DNA fragment (Fragment B) was digested with Xho I and Avr II and purified by preparative gel electrophoresis.

[0092] Plasmid pCJW80 is derived from pCJR24 and DEBS1-TE in which Msc I and Avr II sites have been introduced to flank the AT of the DEBS loading module. This plasmid was digested with Nde I and Avr II and the larger fragment (Fragment C) purified by preparative gel electrophoresis.

[0093] The three fragments (Fragments A, B, C) were ligated together using T4 DNA ligase and the ligation mixture used to transform electrocompetent E. coli DH10B cells. Individual clones were checked for the presence of the desired plasmid pSGK005. The identity of pSGK005 was confirmed by restriction pattern and sequence analysis.

[0094] Plasmid pSGK005 was used to transform S. erythraea NRRL2338 using a routine protoplast transformation technique. Thiostrepton resistant colonies were selected on R2T20 media containing g/ml thiostrepton. Further analysis confirmed that pSGK005 had integrated into the S. erythraea NRRL2338 chromosome by Southern blot hybridisation of their genomic DNA with DIG-labelled DNA containing the actII orf4 promoter. The culture S. erythraea NRRL2338 (pSGK005) was inoculated into 5 ml tap water medium in a 30 ml flask. After three days incubation at 29° C. this flask was used to inoculate 30 ml of Ery-P medium in a 300 ml flask. The broth was incubated at 29° C. at 200rpm for 6 days. After this time the whole broth was adjusted to pH8.5 with NaOH, and then extracted twice with an equal volume of ethyl acetate. The ethyl acetate extract was evaporated to dryness at 45° C. under a nitrogen stream using a Zymark Turbovap LV evaporator. The product identities were confirmed by LC/MS. A peak was observed with a m/z value of 734 (M+H)⁺ required for erythromycin A. A second peak was observed with a m/z value of 748 (M+H)⁺, required for 13-propyl erythromycin A.

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[0150] 51. Wietzorrek, A. and Bibb, M. (1997) A novel family of proteins that regulates antibiotic production in Streptomycetes appears to contain an OmpR-like DNA-binding fold. Molecular Microbiology, 25, 1181-1184.

[0151] 52. Xue, Y. Q., Zhao, L. S., Liu, H. W. and Sherman, D. H. (1998) A gene cluster for macrolide an antibiotic biosynthesis in Streptomyces venezuelae: Architecture of metabolic diversity. Proceedings of the National Academy of Sciences of the United States of America, 95, 12111-12116. TABLE I gene function start end gdhA glutamate dehydrogenase (partial) 1038 0 dapA dihydrodipicolinate synthase 2140 1220 orf3 putative transcriptional activator 2211 3152 orf4 hypothetical protein 3264 3680 orf5 hypothetical protein 4307 3684 orf6 hypothetical protein 4570 4758 orf7 hypothetical protein 5058 5612 acpX acyl carrier protein 6010 5693 ksX ketoacyl synthase 8531 6045 monCI probable epoxihydrolase/cyclase 9542 8643 monE methyltransferase 10426 9596 monT monensin resistance gene (ABC- 10656 12191 monRI probable repressor 12205 12780 monAI thioesterase 13829 13023 monAI polyketide synthase loading & 14121 23198 KS-L 14172 15486 AT-L malonate specific 15777 16880 ACP-L 17019 17276 KS1 17358 18626 AT1 methylmalonate specific 18960 19976 DH1 (potential) 20019 20519 KR1 (inactive) 21636 22241 ACP1 22536 22793 monAI polyketide synthase module 2 23205 29921 KS2 23307 24569 AT2 methylmalonate specific 24891 25913 DH2 25953 26369 ER2 27600 28463 KR2 28485 29042 ACP2 29313 29570 monAI polyketide synthase modules 3 & 4 29974 42372 KS3 30076 31347 AT3 malonate specific 31798 32838 DH3 32884 33465 KR3 34692 35181 ACP3 35553 35811 KS4 35899 37170 AT4 methylmalonate specific 37489 38511 DH4 38557 38982 ER4 40123 40986 KR4 41005 41562 ACP4 41848 42105 monAI polyketide synthase modules 5 & 6 42448 54564 KS5 42628 43890 AT5 ethylmalonate specific 44221 45243 DH5 45289 45744 KR5 46785 47337 ACP5 47593 47850 KS6 47947 49218 AT6 malonate specific 49579 50601 DH6 50644 51075 ER6 52222 53102 KR6 53101 53661 ACP6 54052 54306 monA polyketide synthase modules 7 & 8 54614 66934 KS7 54716 55978 AT7 methylmalonate specific 56300 57319 DH7 57358 57802 KR7 59048 59608 ACP7 59867 60124 KS8 60185 61453 AT8 malonate specific 61808 62839 DH8 62882 63316 ER8 64577 65437 KR8 65456 66016 ACP8 66404 66661 monA polyketide synthase module 9 66952 72054 KS9 67075 68340 AT9 malonate specific 68698 69729 KR9 (potential) 70735 71262 ACP9 71536 71783 monH probable regulator 72051 74993 monCI FAD containing epoxidase 76541 75051 monBI double bond isomerase 76960 76538 monBI double bond isomerase 77450 77016 monA polyketide synthase modules 11 & 88708 77447 KS11 88612 87344 AT11 methylmalonate specific 87022 85993 KR11 85111 84562 ACP11 84292 84035 KS12 83962 82694 AT12 methylmalonate specific 82354 81335 DH12 (potential) delta 81286 80855 ER12 (potential) 79618 78914 KR12 78895 78337 ACP12 78070 77812 monA polyketide synthase module 10 93741 88816 KS10 93636 92368 AT10 methylmalonate specific 92040 91021 KR10 90132 89584 ACP10 89322 89068 monD P450 oxygenase 94081 95273 monRI probable activator 96141 95338 monA thioesterase 96941 96138 orf29 cell wall biosynthesis capK 97580 98953 lipB lipase B 99983 98991 orf31 ion pump 101433 100507 orf32 membrane structural protein 102581 101490 amtA glycine amidinotransferase 102924 103450

[0152] TABLE II GdhA, glutamate dehydrogenase (partial coding sequence) Length: 346 amino acids 1 LTTRPDTKTA LSQKTALSQL LTEIEHRNPA QPEFHQAARE VLETLAPVIA 51 ARPEYAEAGL IERLCEPERQ IVFRVPWQDD HGRVRVNRGF RVEFNSALGP 101 YKGGLRFHPS VNLGVIKFLG FEQIFKNALT GLGIGGGKGG SDFDPRGRSD 151 AEVMRFCQSF MTELYRHIGE HTDVPAGDIG VGGREIGYLF GQYRRITNRW 201 EAGVLTGKGR NWGGSLIRPE ATGYGNVLFA AAMLRERGET LEGRTAVVSG 251 SGNVAIYTIQ KLAALGANAV TCSDSSGYVV DEKGIDLDLL KQVKEVERAR 301 VDTYAQRRGA SARFVPGRRV WEVPADIALP SATQNELDAD DATALI DapA, dihydrodopicolinate synthase Length: 307 amino acids 1 MTLASSLEPT TEPLFNGLYV PLVTPFTDDL RLAPEALARL ADEALSAGAS 51 GLVALGTTAE AATLTAEERE TVIRVCSAAC RAHGAPLIVG VGTNDTATAI 101 TALRELAARG DVAAALVPAP PYIRPGEAGT LAHFAALAEH GGLPLVVYDI 151 PYRTGQTLGA GTITALGRLP EVVGIKHATG SIDPTTMELL DSPLPGFAVL 201 GGDDIVLSPL VAAGAHGGIV ASANLRTADY AEMIALWRRG SAAPARALGA 251 DLARLSAALF TEPNPTVIKG VLHAQNRIPS PAVRMPLLAA SADSVRRAAP 301 LAASRK* ORF3, putative transcriptional activator protein Length: 314 amino acids 1 MLDVRRLHLL RELDRRGTIA AVAEALTFTA SAVSQQLGVL EREAGVPLLE 51 RSGRRVVLTP AGRSLVAHAD AVLNRLEQAV AELAGARDGI GGPLRIGTFP 101 SGGHTIVPGA LAELASRHPA LEPMVREIDS ARVSDGLRAG ELDVALVHDY 151 DFVPATPDTT VDEVPLLEEP MYLVTHAADT ATDSGSGSTL AALLGPCAEV 201 PWITARDGTT GHAMAVRACQ AAGFQPRIRH QVNDFRTVLA LVAAGQGAGF 251 VPRMAAEPSP AGVVLTKLPL FRRSKVAFRA GGGAHPAIAA FVAAATTAVE 301 RMAGSRGPAG GSE* ORF4, hypothetical protein Length: 139 amino acids 1 MADDAYLFLL PDRHPRLGAA LAAVGALECT ETPAVHAWLQ AHEASVSSEQ 51 VRILPADAET LIPKDAERLP VPLSEEEALK VEQECAPQTV TDMESELLAF 101 RETTQDWQAL VHRALTAGIP AQRIARLTGL DPEEIGRL* ORF5, hypothetical protein Length: 208 amino acids 1 LAVAACAAVV LPIDAVVRIS AADVGVLVFF AYLLPYLAIT MTVFVSVAPE 51 QVRSWARREA RGTFLQRYVL GTAPGPGGSL FIAAAALVVA VLWLPGHLST 101 TFSALPRTLV ALALVVAAWI CVVVAFAVTF QADNLVENER ALEFPGERSP 151 AWADYVYFAL AAMTTFGTTD VDVTSRDMRR TVAANTVIAF VFNTVTVAIL 201 VSALGGR* ORF6, hypothetical protein Length: 63 amino acids 1 MTVMDKLKQM LKGHEDKAGQ GIDKAGDFVD GKTQGKYSGQ VDTAQDKLRD 51 QFGSDQQEPP QR* ORF7, hypothetical protein Length: 185 amino acids 1 MGTAQSQEQA AAPGACAAFV RFVLCGGGVG LASSFAVVAL ASWVPWALAN 51 ALVAVVSTVV ATELHARFTF GAGGRATWRQ HAQSAGSAAA AYAVTCVAMF 101 VLQQLVAAPG AVLEQVVYLS ASALAGVARF VVLRLVVFAR NRSLPAAAAV 151 RTARPVRRVP APVPATVAHA ASRPAGPAAL CPAA* AcpX, acyl carrier protein (ACP) Length: 106 amino acids 1 MTSTDHTSGQ DATELEKQLA AATPEEREKL LTDTIRTQAG TLLNTTLSDD 51 SNFLENGLNS LTALELTKTL MTLTGMEIAM VAIVENPTPA QLAHHLGQEL 101 AHTTA* KsX, ketoacyL-ACP synthase Length: 829 amino acids 1 VANEEKLVEY LKWTTAELHQ AQQQLRELKA AQHEPIAVVS MACRLPGKTR 51 TPDDLWDLVS EGRDAVTGFP DDRAWELPEE RPYAELGGFL DDAAGFDAGF 101 FDISDTEAVA TEPLQRLMLH LAWETVERGH IAPHTLRSTL TGVYVGATGH 151 DYATRLETAP DELLPYLGGG TSGSLVSGRI AYALGLEGPA ISVDTACSSS 201 LVALHLLACQA LRRGECGLAL AGGGTVMSTP HTFHAFAHQK SLAQDGRCKP 251 FAAAADGMGL GEGVGLVLLE RLGDARKNGH PVLAVIRGSA VNQDGAGYGL 301 AAPNGPSQQH VTRAALADAG LTPDQIDAVE AHGTGTPIGD AIEVQALLAT 351 YGADRSPDRP LWLGSVKSNT GHTQGAAGAA ALIKMVQAFR HGTLPPTLHV 401 DRPTPLAAWK KGAVRLLTEA VDWPRREEPR RVGISAFATS GTNAHLILEE 451 PPVDEAPVPD AARDQTSPVA PELPVAWSLS ARTPEALRAQ AKALVTHLAA 501 TDPAPSPAEV AYSLAATRSP LEHRAVLTGT DHTELLAAAR ALAAGEDHPD 551 LVRSTPGAGP KKIAWHFDGR PADGVTTGAA PGAKPGATFG ATFGAAFGGA 601 EFHSAFPLFA SAFDEARALL DTHLPTPLPT PHSELARFAV HTALARLLLE 651 TGVRPHTLTG DGVGHIAAAY AAGILTLDDA CRLAAAHAAA AQAAEGEQPA 701 PPDAYEPVLK QLTFQRATLT LTSTAPADTP IASADYWHHH LTSPAPTAPP 751 TPETHTLLHL GALSPEGTQT SAVSALLTAL ARLHTTGGTV DWTPLVRRTP 801 HPRTIDLPTY SFQATRYWLH DHTAHAAV* MonCII, probable epoxyhydrolase/cyclase Length: 300 amino acids 1 VKNLRIPVSQ TVSLNVRYRP ADGPGAPGRP FLLLHGMLSN ARMWDEVAAR 51 LAAAGHPAYA VDHRGHGESD TPPDGYDNAT VVTDLVAAVT ALDLSGALVA 101 GHSWGAHLAL RLAAEHPDLV AGLALIDGGW YEFDGPVMRA FWERTADVVR 151 RAQQGTTSAA DMRAYLRATH PDWSPTSIEA RLADYRVGPD GLLIPRLTST 201 QVMSIVAGLQ REAPADWYPK VTVPVRLLPL IPAIPQLSDQ VRAWVAAAEA 251 ALEQVSVRWY PGSDHDLHAG APDEIAADLL LLARSCEAMP GGKAGVRPA* MonE, S-adeonosylmethionine-dependent methyltransferase Length: 277 amino acids 1 VNKTVAPEPS DIGHYYDHKV FDLMTQLGDG NLHYGYWFDG GEQQATFDEA 51 MVQMTDEMIR RLDPAPGDRV LDIGCGNGTP AMQLARARDV EVVGISVSAR 101 QVERGNRRAR EAGLADRVRF EQVDAMNLPF DDGSFDHCWA LESMLHMPDK 151 QQVLTEAHRV VKPGARMPIA DMVYLNPDPS RPRTATVSDT TTYAALTDIG 201 DYPDIFRAAG WTVLELTDIT RETAKTYDGY VEWIRAHRDE YVDIIGVEGY 251 ELFLHNQAAL GKMPELGYIF ATAQRP* MonT, putative monensin resistance gene (ABC-transporter) Length: 512 amino acids 1 MSADLGARRW WAVGALVLAS MVVGFDVTIL SLALPAMADD LGANNVELQW 51 FVTSYTLVFA AGMIPAGMLG DRFGRKKVLL TALVIFGIAS LACAYATSSG 101 TFIGARAVLG LGAALIMPTT LSLLPVMFSD EERPKAIGAV AGAAMLAYPL 151 GPILGGYLLN HFWWGSVFLI NVPVVILAFL AVSAWLPESK AKEAKPFDIG 201 GLVFSSVGLA ALTYGVIQGG EKGWTDVTTL VPCIGGLLAL VLFVMWEKRV 251 ADPLVDLSLF RSARFTSGTM LGTVINFTMF GVLFTMPQYY QAVLGTDAMG 301 SGFRLLPMVG GLLVGVTVAN KVAKALGPKT AVGIGFALLA AALFYGATTD 351 VSSGTGLAAA WTAAYGLGLG IALPTAMDAA LGALSEDSAG VGSGVNQSIR 401 TLGGSFGAAI LGSILNSGYR GKLDLDGVPE QAHGAVKDSV FGGLAVARAI 451 KSNGLADSVR SAYVHALDVV LVVSGGLGLL GVVLAVVWLP RHVGQSTAKT 501 AESEHEAADA V* MonRII, probable repressor protein Length: 192 amino acids 1 VPGLRERKKA RTKAAIQREA VRLFREQGYT ATTIEQIAEA AEVAPSTVFR 51 YFATKQDLVF SHDYDLPFAM MVQAQSPDLT PIQAERQAIR SMLQDISEQE 101 LALQRERFVL ILSEPELWGA SLGNIGQTMQ IMSEQVAKRA GRDPRDPAVR 151 AYTGAVFGVM LQVSMDWAND PDMDFATTLD EALHYLEDLR P* MonAIX, thioesterase Length: 269 amino acids 1 MDRGTAARAP QIGDEFGAAT GNGVWLRRYH AAAEAPVRLV CFPFAGGSAS 51 YYFGLSGLLA PGVEVLAVQY PCRQDRHAEP CLASVAELAD GVVPHLPCDG 101 KPFALFGHSL GAIVAFEVAR RLRGPAGPGL PVHLFVSGGL ARPYRPAGRS 151 GAFGDADILA HLRAMGGTDE RFFRSPELQE LVLPALRADY RAVATYEAPG 201 PGRLDCPITA LIGDADERTS PEQAATWRER TGAAFDLRVL PGGHFYLDGC 251 QEQVAAVVTE ALTAGPGV* MonAI, polyketide synthase multi-enzyme MONS1, housing loading module and extension module 1 Length: 3026 amino acids 1 MAASASASPS GPSAGPDPIA VVGMACRLPG APDPDAFWRL LSEGRSAVST 51 APPERRRADS GLHGPGGYLD RIDGFDADFF HISPREAVAM DPQQRLLLEL 101 SWEALEDAGI RPPTLARSRT GVFVGAFWDD YTDVLNLRAP GAVTRHTMTG 151 VHRSILANRI SYAYHLAGPS LTVDTAQSSS LVAVHLACES IRSGDSDIAF 201 AGGVNLICSP RTTELAAARF GGLSAAGRCH TFDARADGFV RGEGGGLVVL 251 KPLAAARRDG DTVYCVIRGS AVNSDGTTDG ITLPSGQAQQ DVVRLACRRA 301 RITPDQVQYV ELHGTGTPVG DPIEAAALGA ALGQDAARAV PLAVGSAKTN 351 VGHLEAAAGI VGLLKTALSI HHRRLAPSLN FTTPNPIAPL ADLGLTVQQD 401 LADWPRPEQP LIAGVSSFGM GGTNGHVVVA AAPDSVAVPE PVGVPERVEV 451 PEPVVVSEPV VVPTPWPVSA HSASALRAQA GRLRTHLAAH RPTPDAARVG 501 HALATTRAPL AHRAVLLGGD TAELLGSLDA LAEGAETASI VRGEAYTEGR 551 TAFLFSGQGA QRLGMGRELY AVFPVFADAL DEAFAALDVH LDRPLREIVL 601 GETDSGGNVS GENVIGEGAD HQALLDQTAY TQPALFAIET SLYRLAASFG 651 LKPDYVLGHS VGEIAAAHVA GVLSLPDASA LVATRGRLMQ AVRAPGAMAA 701 WQATADEAAE QLAGHERHVT VAAVNGPDSV VVSGDRATVD ELTAAWRGRG 751 RKAHHLKVSH AFHSPHMDPI LDELRAVAAG LTFHEPVIPV VSNVTGELVT 801 ATATGSGAGQ ADPEYWARHA REPVRFLSGV RGLCERGVTT FVELGPDAPL 851 SAMARDCFPA PADRSRPRPA AIATCRRGRD EVATFLRSLA QAYVRGADVD 901 FTRAYGATAT RRFPLPTYPF QRERHWPAAA CVGQQPETPE LPESSESSEQ 951 AGHEREEGAR AWGGPEGRLA GLSVNDQERV LLGLVTKHVA VVLGDASGTV 1001 QAARTFKQLG FDSMAAAELS ERLGTETGLP LPATLTFDYP TPLAVAAHLR 1051 AELTGTPAPA GSAPATGALG AGDLGTDEDP VAIVAMSCRY PGGAGTPEDL 1101 WRLVAGGADA IGDFPTDRGW DLARLFHPDP DRSGTSCTRQ GGFLYDAADF 1151 DAEFFDISPR EALAVDPQQR LLLECAWEAF ERAGLDPRAL KGSPTGVFVG 1201 MTGQDYGPRL HEPSQATDGY LLTGSTPSVA SGRLSFSFGL EGPALTVDTA 1251 CSSSLVTLHL AAQALRRGEC DLALAGGATV LATPGMFTEF SRQRGLAPDG 1301 RCKPFAAGAD GTGWAEGVGL VLLERLSEAR RKGHAVLAVI RGSAINQDGA 1351 SNGLTAPNGP SQQRVIRAAL AAARLTADEV DVVEAHGTGT TLGDPIEAQA 1401 LLATYGQGRS AERPLWLGSV KSNIGHTQAA AGVAGVIKMV MAMRHDLLPA 1451 TLHVDEPSGH VDWSTGAVRL LTEPVVWPRG ERPRRAAVSS FGISGTNAHL 1501 VLEEAGQDEY VAGAADDAGP VDGAVLPWVV SGRTGAALRE QARRLRELVT 1551 GGSADVSVSG VGRSLVTTRA VFEHRAVVVG RDRDTLIGGL EALAAGDASP 1601 DVVCGVAGDV GPGPVLVFPG QGSQWVGMGA QLLGESAVFA ARIDACEQAL 1651 SPYVDWSLTE VLRGDGRELS RVDVVQPVLW AVMVSLAAVW ADHGVTPAAV 1701 VGHSQGEIAA VVVAGALTLE DGAKIVALRS RALRQLSGGG AMASLGVGQE 1751 QAAELVEGHP GVGIAAVNGP SSTVISGPPE QVAAVVADAE ARELRGRVID 1801 VDYASHSPQV DAITDELTHT LSGVRPTTAP VAFYSAVTGT RIDTAGLDTD 1851 YWVTNLRRPV RFADAVTALL ADGHRVFIEA SSHPVLTLGL QETFEEAGVD 1901 AVTVPTLRRE DGGRARLARS LAQAFGAGCA VRWENWFPAT GTSTVELPTY 1951 AFQRRRYWLE APTGTQDAAG LGLAAAGHPL LGAATEIAIDG DIRLLTGRIS 2001 RHSHPWLAQH TLFGAAVVPA SVLAEWALRA ADEAGCPRVD DLTLRTPLVL 2051 PETAGVQVQI VVGPADARDG HRDFHVYARP DGKDASEGEG IAEGEGASEG 2101 EGASGGTDAP WTCHADGRLV AEPTGTASED SPDTVWPPPG AEPVDLGDFY 2151 ERAAATGVGY GPVFTGLRAL WRRDGELFAE AVLPQEAPET AGFGMHPALL 2201 DAALHPALLG ERPAEEDKVW LPFTLTGVTL WATGATSVRV RLTPLDDDPD 2251 ASADGRAWRV GVSDPTGAEV LTCEALVAVA AGRRELRAAG ERVSDLYAVE 2301 WVPVPGPGPV GEGADFSGWA GLGECGERWE CVGRVERWYE DLDALGAAVE 2351 GGASVPSVVL ATAAAAPGGA GDGAADALSA VRWTGALLDQ WLADARFADA 2401 RLVVITSGAV ATGDDFLPDP AAAAVRGLVE QAQVRHPGRI LLVDTEAGAG 2451 LGVGAGVDDA LLEQAVAMAL GADEPQLALR AGRVLAPRLT APQDAAVTEA 2501 ARPLDPDGTV LITGPAGAPV ADLAEHLVRT GQCRHLLLLP GDGELEEMAE 2551 ELRGLGATVD LSTADPADPT ALAEVVAAVE GDHPLTGVIH ATGVVDAFDP 2601 GDSASDLMID SASDSFAEAW SSRAGVTAAL HTATAHLPLD LFAVLSPAGA 2651 DLGIARSAAA AGADAFSAAL ALRRHTTVTT DTTAPPRTTA PPRTTASPRT 2701 TALSSSRTTG VALAYGPPTA PRPGIKGTAP GRIPVLLDAA RAHGGGSPLL 2751 GARLAARALA AESAAEGVAG LPAPLRALAV AAAAAGAPTR RTAADRKPPA 2801 DWPARLAPLS APEQLRLLID AVRTHAAAVL GRTDPEALRG DATFKQLGLD 2851 SLTAVELRNR LVEDTGLRLP TALVFRYPTP AAIAAHLRER LTSPSETTAT 2901 QRSGGQTPAA GQASSALAPG GSAAGPPAAD TVLSDLTRME NTLSVLAAQL 2951 PHTETGEITT RLEALLTRWK TTNATANDSG DGNGGDDDAA ERLKAASADQ 3001 IFDFIDNELG VGHGTSRVTP TPKAG* MonAII, polyketide synthase multi-enzyme MONS2, housing extension module 2 Length: 2239 amino acids 1 MASEEQLVEY LRRVTTELHD TRRRLVQEED RRQEPVALVG MACRFPGGVA 51 SPEDLWDLVA AGKDAIEDFP TDRGWDLEAL YDPDPAAYGT SYVRHGGFVD 101 DAGSFDADFF GISPREALAM DPQQRLMLET SWELFERAGI EPVSLKGSRT 151 GVYAGVSSED YMSQLPRIPE GFEGHATTGS LTSVISGRVA YNYGLEGPAV 201 TVDTACSASL VAIHLASQAL RQRECDLALA GGVLVLSSPL MFTEFCRQRG 251 LAPDGRCKPF AAAADGTGFS EGIGLLLLER LSDARRNGHK VLAVIRGSAV 301 NQDGASNGLT APNDAAQEQV IRAALDNARL TPSEVDAVEA HGTGTKLGDP 351 IEAGALLATY GQHRARPLLL GSLKSNIGHT HATAGVAGVI KTVMAIRNGL 401 LPATLHVEEL SPHVDWDAGA VEVVTEPTPW PETGHPRRAG VSAFGISGTN 451 AHLILEEAPP EEDVPAPVVV ESGGVVPWVV SGRTPEALRE QARRLGEFVA 501 GDTDALPNEV GWSLATTRSV FEHRAVVVGR DRDALTAGLG ALAAGEASAG 551 VVAGVAGDVG PGPVLVFPGQ GAQWVGMGAQ LLDESAVFAA RIAECERALS 601 AHVDWSLSAV LRGDGSELSR VEVVQPVLWA VMVSLAAVWA DYGVTPAAVI 651 GHSQGEMAAA CVAGALSLED AARIVAVRSD ALRQLQGHGD MASLSTGAEQ 701 AAELIGDRPG VVVAAVNGPS STVISGPPEH VAAVVADAEA RGLRARVIDV 751 GYASHGPQID QLHDLLTERL ADIRPTNTDV AFYSTVTAER LTDTTALDTD 801 YWVTNLRQPV RFADTIEALL ADGYRLFIEA SAHPVLGLGM EETIEQADMP 851 ATVVPTLRRD HGDTTQLTRA AAHAFTAGAD VDWRRWFPAD PAPRTIDLPT 901 YAFQRRRYWL ADTVKRDSGW DPAGSGHAQL PTAVALADGG VVLNGRVSAE 951 RGGWLGGHVV AGTVLVPGAA LVEWVLRAGD EAGCPSLEEL TLQAPLVLPE 1001 SGGLQVQVVV GAADEQGGRR DVHVYSRSEQ DASAVWQCHA VGELGRASVA 1051 RPVRQAGQWP PAGAEPVEVG GFYEGVAAAG YEYGPAFRGL RAMWRHGDDL 1101 LAEVELPEEA GSPAGFGIHP ALLDAALHPL LAQRSRDGAG AGAHGGQVLL 1151 PFSWSGVSLW ASEATTVRVR LTGLGGGDDE TVSLTVTDPA GGPVVDVAEL 1201 RLRSTSARQV RGSAGPGADG LYELRWTPLP EPLPVPAPAN GRDVAADLSG 1251 CAVLGELVAE PGPGIDLEGC PCYPGVGALA DNASPPSMIL APVHSDTTGG 1301 DGLALTERVL RVIQDFLAAP SLEQKQTRLA FVTRGAADTG STTGGSAAPA 1351 EAVDPAVAAV WGLVRSAQSE NPGRFVLLDT DAPLDQASVA PLVDAVRSAV 1401 EADEPQVALR GGRLLVPRWA RAGEPVELAG PAGARAWRLV GGDSGTLEAV 1451 VAEACDDIVL RPLAPGQVRV AVHTAGVNFR DVLIALGMYP DPDALPGTEA 1501 AGVVTEVGPG VTRLSVGDRV MGMMDGAFGP WAVADARMLA PVPPGWGTRQ 1551 AAAAPAAFLT AWYGLVELAG LKAGERVLIH AATGGVGMAA VQIARHVGAE 1601 VFATASPGKH AVLEEMGIDA AHRASSRDLA FEDAFRQATD GRGVDVVLNS 1651 LTGELLDASL RLLGDGGRFV EMGKSDPRDP ELVALEHPGV SYEAFDLVAD 1701 AGPERLGLML DRLGELFAGG SLVPLPVTAW PLGRAREALR HMSQARHTGK 1751 LVLDVPAPLD PDGTVLVTGG TGTIGAAVAE HLARTGESKH LLIVSRSGPA 1801 AHGAEELVSR IAEFGAEATF VAADVSEPDA VAALIEGIDP AHPLTGVVHA 1851 AGVLDNALIG SQTTESLTRV WAAKAAAAQQ LHEATRESRL GLFVMFSSFA 1901 STMGTPGQAN YSAANAYCDA LAALRRAEGL AGLSVAWGLW EATSGLTGTL 1951 SAADRARIDR YGIRPTSAAR GCALLAAARA HGRPDLLAMD LDARVPAASD 2001 APVPAVLRTL AAAGAPATAR PTAAAAADGA TDWSGRLAGL TEEARLELLT 2051 ELVCTHAAGV LGHADAGAVQ VDAPFKELGF DSLTAVELRN RIAAATGLKL 2101 PAALVFDYPQ ARVLAAHLAE RLVPEGAGAM GGVSGAEGVR DAYGAGGPGG 2151 DMTAQVLLEV ARVEHTLSAA VPHGLDRAAV AARLEALLAR CTATTAATGA 2201 AGAAVEGDGD SDGDGAVDQL ETATAEQVLD FIDNELGV* MonAIII, polyketide synthase multi-enzyme MONS3, housing extension modules 3 and 4 Length: 4133 amino acids 1 MVSEEKLVDY LKRVSADLHA TRQRLREAEE RGQEPVAVVE AACRYPGGIR 51 TPEDLWDLVA AGGNALGAFP DNRGWDLRRL FHPDPDHPGT TYAREGGFLH 101 DADLFDPEFF GISPREAAVL DPQQRLLLEC AWEALERAGI DPRSLQGSRT 151 GVYAGAALPG FGTPHIDPAA EGHLVTGSAP SVLSGRLAYT FGLEGPAVTI 201 DTACSSSLVA VHLAAHALRQ RECDLALAGG VTVMTTPYVF TEFSRQRGLA 251 ADGRCKPFAA AADGTAFSEG AGLLVLERLS DARRAGHRVL AVIRGSAVNQ 301 DGASNGLTAP NGPAQQRVIR AALAGARLSP AEVDAVEAHG TGTRLGDPIE 351 ADALLATYGQ ERHGGRPLWL GSVKSNIGHT QGAAGAAGLI KMVQALRHET 401 LPATLYADEP TPHADWESGA VRLLSAPVAW PRGEHGEHTR RAGISSFGIS 451 GTNAHLILEE APAADAEGAG GDGDGDGGGV RPVVRVGATG PREEQGQGQG 501 QEQHQQQRQQ RQRSSMMPTP HLPWLLSARS PAALRAQADA LANHVAHADH 551 SIADIGGTLL RRTLFEHRAV VLGTDRDERA AALAALAAGR AHPALTRAAG 601 PARNGGTAFL FTGQGSQRPG MGRQLYDTFD VFAESLDETC ARLDPLLEQP 651 LKPVLFAPAD TAQAAVLHGT GMTQAALFAL EVALYRQVTS FGIAPSHLTG 701 HSVGEIAAAH VAGVFSLADA CTLVAARGRL MQALPAGGAM LAVQAAEDDV 751 LPLLAGQEER LSLAAVNGPT AVVVSGEAAA VGEVEKALRG RGLKTKRLNV 801 SHAFHSPLIE PMLDDFREVA RGLTFHAPTL PVVSNLTGRL ADAELMADAE 851 YWVRHVRRPV RFHDGLRALS EQGVVRYLEL GPDPVLATMV QDGLPAPAEG 901 EEPEPVVAAA LRSKHDEGRT LLGAVAALHT DGQPADLTAL FPADAGQVPL 951 PTYRFQRRRY WRVAPDAAAP ARAAGLQETG HPLLPAVIRQ ADGGILLAGR 1001 LSLRTHPWLA DHTIAGGVPL PATAFVELAL LAGRHAACDT IDDLTLETPL 1051 LLDDTGTGVG AAVGAGADAL VDAIEVQLAL GAPDGSGRRA LTVHSRPADD 1101 AADDGDAADA ADAAGRGGPG GSGDLGDPGD PGDLGDGGGS RGWRRHATGI 1151 LSAGPAAEPA APDAAPWPPA DATALDVDAL YARLDAQGYS YGPAFRAVHA 1201 AWRHGDDLYA DVRLADEQRA EADAFALHPA LLDAALHAVD ELYRGSEGRC 1251 QEQGQGGQEP EQGRGDADAP VRLPFSFSDI RHHATGATRL WVRLSPQGDD 1301 RLRLSLTDGE GGQVATVDAL QLRLIPADRW RAARPTTAAP LYHLDWHELP 1351 LPEPAETDPA AHSWAVLGAH DAGLAPAAHY PDLAALKAAV EAGEPVPDIV 1401 FAPFPAQGTE TDVPAQVRAH ARHALELLRD WLTTEAFAAA RLVVLTTGAV 1451 TARPEDGPAD LATAPVWGLV RAAQAEQPDH VVLVDIDKDI DKDTDEETDQ 1501 ATDAGTASRH ALPAALAAAA AQAETQLALR AGTVLVPRLA VVPPRTDTPA 1551 LHATAPESTT DTVDSTGIAG AAESGGTVLI TGGTGGLGQA VARHLAAAHG 1601 ARHLLLVSRR GDAAEGVAEL RADLADDGVD VRVAACDITD RDALAGLLAD 1651 IPAAHPLTAV VHTAGVIDDS LITAMTPERL DAVLAPKADA AWHLHELTRD 1701 KDLSAFVLFS SGASVLGNGG QANYAAANTF LNTLAEHRRA AGLAATSVAW 1751 GLWESASGGM AARLGDADA RIHRTGVTGL TDEQALALFD AALTAEIIPTV 1801 LATRFDRAVL RGQAAARTLQ PALRGLVRTP RPTASAGAIG STAATGSATD 1851 ENAPSSWAAR LARLSAADRD RALNELIREQ IATVLAHPSP DTIELGRAFQ 1901 ELGFDSLTAL ELRNRLSTAT GIRLPATLVF DHPSPTALVR HLHSHLPDEA 1951 QHTSPTAPGA SAEGTAATAT GIDDDPIAIV GMACRYPGGV TSPEQLWQLV 2001 ATGTDAIGPF PEDRGWDTAG LFDPDPDQVC HSYTREGGFL YDAARFDAGF 2051 FGISPREAAA TDPQQRLLLE TAWQAFEHAG IDPAALRGTP CGVITGIMYD 2101 DYGSRFLARK PDGFEGRIMT GSTPSVASGR VAYTFGLEGP AITVDTACSS 2151 SLVAMHLAAQ ALRQGECELA LAGGVTVMAT PNTFVEFSRQ RGLAPDGRCK 2201 PFAAAADGTG WGEGAGLVVL ERLSDARRKG HRVLALLRGS AVNQDGASNG 2251 MTAPNGPSQE RVIRTALAGA GRGPEDIDVV EAHGTGTTLG DPIEAQALLA 2301 TYGQGRPEDR PLWLGSVKSN IGHTQAAAGV AGVIKMVMAL RHEQLPTTLH 2351 ADEPTPHVQW DGGGVRLLTE PVPWSRGERT RRAGVSSFGI SGTNAHLILE 2401 EPPEEDLPEP VAAEPGGVVP WVVSGRTPDA LREQARRLGE FVVGAGDVSA 2451 AEVGWSLATT RSVFEHRAVV AGRDRDDLVA GMQALAAGET PTDVVSGAAA 2501 SSGAGPVLVF PGQGSQWVGM GAQLLDESPV FAARIAECEQ ALSAYVDWSL 2551 SDVLRGDGSE LSRVEVVQPV LWAVMVSLAA VWADYGVTPA AVVGHSQGEM 2601 AAACVAGALS LEDAARIVAV RSDALRQLQG HGDMASLGTG AEQAAELIGD 2651 RPGVVVAAVN GPSSTVISGP PEHVAAVVAE AEARGLRARV IDVGYASHGP 2701 QIDQLHDLLT EGLADIRPAN TDVAFYSTVT AERLTDTTAL DTDYWVTNLR 2751 QPVRFADTIE ALLADGYRLF IEASAHPVLG LGMEETIEQA DIPATVVPTL 2801 RRDHGDTTQL TRAAAHAFTA GADVDWRRWF PADPTPRTVD LPTYAFQHQH 2851 YWLEEPSGLT GDAADLGMVA AGHPLLGACV ELAESDSYLF TGRLSRRAPS 2901 WLAEHVVAGT VLVPGAALVE WVLRAGDEAG CPTIEELTLQ APLVLPESGG 2951 LQVQVVVGAT DEQSGRRDVH VYSRSEQDAS AVWVCHAVGV VSSEMPEAAA 3001 ELSGQWPPAG AEAVDVEDFY ARAAEAGYAY GPAFQGLRAL WRHGTELFAE 3051 VVLPEQAGGH DGFGIHPALL DAALHPLMLL DRPADGQMWL PFAWSGVSLN 3101 ADRATHVRVR LSPRGEAAER DLRVVIADAT GAPVLTVDAL TLRAADPGRL 3151 GAAARGGVDG LYTVDWTPLP LPQPLPLPRT DAGGSADWVI LSDNSSAALA 3201 DAVSSATAAG GGAPWALLAP VGGGSADDGL PVVRRTLSLV QEFLAAPELT 3251 ESRLVIVTRG AVATDADGDV AASAAAVWGL IRSAQSENPG RFVLLDVEEE 3301 HLHPDGGELP YAALRHAVEE LDEPQLALRS GKFLVPRMTP AAAPEELVPP 3351 VGTSGWRLGT SGTATLENLS VIDAPEAFAP LEPGQVRISV RAAGMNFRDV 3401 LIALGMYPDK GTFAGSEGAG HVTEVGPGVT HLSVGDRVMG LFEGAFAPLA 3451 VADARMVVPI PEGWSFQEAA AVPVVFLTAW YGLVDLGRLR AGESLLIHAG 3501 TGGVGMAATQ IARHLGAEVF ATASPAKHGV LDGMGIDAAH RASSRDLDFE 3551 ETLRAATGGR GMDVVLNSLA GEFTDASLRL LAEGGRMVDM GKTDKRDPDR 3601 VAAEHAGAWY RAFDLVPHAG PDRIGEMLAE LGELFASGAL APLPVQTWPL 3651 GRAREAFRFM SQAKHTGKLV LEIPPALDPD GTVLITGGTG VLAAAVAEHL 3701 VREWGVRHLL LAGRRGSEAP GSSELAEELT ELGAEVTFAA ADVSDPDAVA 3751 ELVGKTDPAH PLTGVIHAAG VLDDAVVTAQ TPESLARVWA AKATAAHLLH 3801 EATREARLGL FLVFSSAAAT LGSPGQANYA AANAYCDALV RQRREAEGLAG 3851 LSIGWGLWQT ASGMTGHLGE TDLARMKRTG FTPLTTEGGL ALLDAARAHG 3901 RPHVVAVDLD ARAVAAQPAP SRPALLRALA AGATPGARTA RRTAAAGSVA 3951 PAGGLADRLA GLPHPERRRL LLDLVRGNVA GVLGHSDHDA VRPDTSFKEL 4001 GFDSLTAVEL RNRLAAATGL KLPAALVFDY PESATLVDHL LERLSPDGAP 4051 PPVKDAADPV LNDLGRIESS LDALALDADA RSRVTRRLNT LLSKLNGAAT 4101 AGSPADVTDL DALDALDDVS DDEMFEFIDR EL* MonAIV, polyketide synthase multi-enzyme MONS4, housing extension modules 5 and 6 Length: 4039 amino acids 1 MSSAEESSPD VSGTGVSGTG ESATGTSSTE AKLRQYLKRV TVDLGQARRR 51 LREVEERAQE PIAIVSMACR FPGDTRTPEA LWDLVAEGGD AIDDFPTNRG 101 WDLESLYHPD PDHPGTSYVR RGGFLYDAPA FDASFFGISP REALAMDPQQ 151 RVLMETAWQL LERAGIDPAS LKLSATGVYI GAGVLGFGGA QPDKTVEGHL 201 LTGSALSVLS GRISFTLGLE GPSVSVDTAC SSSLVSMHLA AQALRQGECD 251 LALAGGVTVM STPGAFTEFS RQGALSPDGR SKAFAASADG TGFSEGAGLL 301 LLERLSDARR NGHKVLAVIR GSAVNQDGAS NGLTAPNGPS QERVIRAALA 351 NAGLGAAEVD AVEAHGTGTK LGDPIEAGAL LATYGRDRDE DRPLWLGSVK 401 SNIGHPQGAA GVAGVIKMVM ALQRELLPAT LYVDEPTPHV DWSSGSVRLL 451 TEPVPWTRGE RPRRAGVSAF GMSGTNAHVI LEEAPPEEAA AAETPAEGTG 501 AVVPWVVSGR GEEALRAQAA QLAEHVRDDD QRPASPLEVG WSLATTRSVF 551 ENRAVVVGDD RDALLDGLRS LAAGEASPDV VSGAVGPTGP GPVMVFPGQG 601 GQWVGMGARL LDESPVFAAR IAECEQALSA YVDWSLTDVL RGDGSELARI 651 DVVQPVLWAV MVALAAVWAD QGIEPAAVVG HSQGEIAAAC VVGAISLDEA 701 ARIVAVRSVL LRQLSGRGGM ASLGMGQEQA ADLIDGHPGV VVAAVNGPSS 751 TVISGPPEGI AAVVADAQER GLRARAVASD VAGHGPQLDA ILDQLTEGLA 801 GIRPAATDVA FYSTVTAGHL TDTTELDTAY WVRNVRRTVR FADTIDALLA 851 DGYRLFIEVS PHPVLNLALE GLIERAAVPA TVVPTLRRDH GDTTQLARAA 901 AHAFAAGADV DWRRWFPADP APRTVDLPTY APQRQDFWPA PAGGRSGDPA 951 GLGLAASGHP LLGASVGLAS GDVHLLSGRV SRQSAAWLDD HVVAGQALVP 1001 GAAQVEWVLR AGDDAGCSAL EELTLQTPLV LPDTGGLRIQ VVVEAADAHG 1051 RRDVRLFSRP DDDDAFASTH PWTCHATGVL APAPTDGTNG TRDAADTLDG 1101 AWPPADAEPV PADDLYAQAD RTGYGYGPAF RGVRALWRHG KDVLAEVTLP 1151 KEAGDPDGFG IHPALLDAVL QPAALLLPPT DAEQVWLPFA WNDVALHAVR 1201 ATTVRVRLTP LGERIDQGLR ITVADAVGAP VLTVRDLRSR PTDTGRLAAA 1251 ATRDRHGLFD LEWIAPENAA ENAAGPARDA SEGWVTLGED AASLADLLAS 1301 VEAGAPAPQL VAAPVEPDRT DDGLALATHV LDLVQTWLAS PLHDSRLVLV 1351 TRGAVTDADV DVAAAAVWGL VRSAQSEHPG RFTLIDLGPD DTLAAAMQAA 1401 HLEEPQLAVH GGEIRVPRLV RATTDPTAPN GTPEADRTAD PSEGLHRNGT 1451 VLITGGTGVL GRLVAEHLVT EWGVRHLLLA SRRGDQAPGS AELRARLSEL 1501 GASVEIAPAD VGDAEAVAAL IASVDPAHPL TGVIHAAGVL DDAVITAQTP 1551 ESLARVWATK ATAARHLHEA TRETPLDFFV VFSSAAASLG SPGQANYAAA 1601 NAYCDALVQH RRAQGLAGLS IAWGLWQATS GMTGQLSETD LARMKRTGFA 1651 ALTDEGGLAL LDAARAHDRA YVVAADLDPR AVTDGLSPLL RALTAPATRR 1701 RVASEGLADG ALATRLAGLD ADGRLRLLTD VVREYVAAVL GHGSAARVGV 1751 DIAFKDLGFD SLTAVELRNR LSAACDVRLP ATLIFDHPTP QALATHLVDR 1801 LAGSTSATTT VNATAPAAAH VAAGADVDAD TDDPVAIVAM TCRFPGGVAS 1851 PDDLWDLLDA RKDAMGAFPT DRGWDLERLF HPDPDHPGTS YTDQGGFLPD 1901 AGDFDAAFFG INPREALAMD PQQRLLLEAS WEVLERAGID PTTLKGTPTG 1951 TYVGLMYHDY AKSFPTADAQ LEGYSYLAST GSMVSGRVAY TLGLEGPAVT 2001 VDTACSSSLV SIHLATQALR HGECDLALAG GVTVMADPDM FAGFSRQRGL 2051 SPDGRCKAYA AAADGVGFSE GVGVLLLERL SDARRHGRRV LGVVRGSAVN 2101 QDGASNGLTA PNGPSQERVI RQALASGGLS SVDVDVVEGH GTGTTLGDPI 2151 EAQALLATYG QGRPEDRPLW LGSVKSNIGH TQAAAGVAGV IKMVMANRHG 2201 VVPASLHVDV PSPHVEWDSG AVRLAVESVP WPQVEGRPRR AGVSSFGASG 2251 TNAHVIVESV PDGLEEDSVS VGGEALETET DGRLVPWVVS ARSPQALRDQ 2301 ALRLRDFASD ASFRAPLADV GWSLLKTRAL HEHRAVVVGA ERAELIAALE 2351 ALATGEPHAA LVGPACSQAR VGGDDVVWLF SGQGSQLVGM GAGLYERFPV 2401 FAAAFDEVCG LLEGPLGVEA GGLREVVFRG PRERLDHTVW AQAGLFALQV 2451 GLARLWESVG VRPDVVLGHS IGEIAAAHVA GVFDLADACR VVGARARLMG 2501 GLPEGGAMCA VQATPAELAA DVDGSAVSVA AVNTPDSTVI SGPSDEVDRI 2551 AGVWRERGRK TKALSVSHAF HSALMEPMLA EFTEAIRGVK FRQPSIPLMS 2601 NVSGERAGEE ITDPEYWARH VRNAVLFQPA IAQVADSAGV FVELGPAPVL 2651 TTAAQHTLDE SDSQESVLVA SLAGERPEES AFVEAMARLH TAGVAVDWSV 2701 LFAGDRVPGL VELPTYAFQR ERFWLSGRSG GGDAATLGLV AAGHPLLGAA 2751 VEFADRGGCL LTGRLSRSGV SWLADHVVAG AVLVPGAALV EWALRAGDEV 2801 GCVTVEELML QAPLVVPEAS GLRVQVVVEE AGEDGRRGVQ IYSRPDADAV 2851 GGDDSWICHA TGVLSPESAR LDTELGGVWP PAGAEPLDVD GFYAQAGEAG 2901 YGYGPAFRGL RAVWRHGQDL LAEVVLPEAA GAHDGYGIHP ALLDATLHPL 2951 LAARFMDGSE DDQLYVPFGW AGVSLRAVGA TTVRVRLRPV GESVDQGLSV 3001 TVTDATGGPV LSVDSLQTRP VKPSQLAAAQ QPDVRGLFTV EWTPLPQTDA 3051 DGEADWVVLS DGVGRLADVV SAAGGEAPWA VVAPVDASVG DGREGLDGRL 3101 VVERVLSLVQ EFLALPELAE SRLLVVTRGA VATGVDGDGD VDASAAAVWG 3151 LVRSAQSENP GRFILLDVDG DGDDQGPDLN GRHLPHATLR HAAEELDEPQ 3201 LALREGTLYV PRLTQARQSA ELVVPPGEPA WRLRMVHDGS LDALAAVACP 3251 EALEPLAPGQ VRIAVHAAGI NFRDVLVALG MVPAYGANGG EGAGVVTEVG 3301 PEVTHVSVGD RVMGVFEGAF GPVVIAEARM VTPVPQGWDM REAAGIPAAF 3351 LTAWYGLVEL AGLKAGERVL VHAATGGVGM AAVQIARHVG AEVFATASPG 3401 KHAVLEEMGI DAAHRASSRD LAFEGTFREA TGGRGMDVVL NSLAGEFIDA 3451 SLRLLGDGGR FLEMGKTDVR AAEEVAAEHA DVSYTAYDLV GDAGPDRISN 3501 MLDKLVELFA SERLKPLPVR SWPLDKAQEA FRFMSQAKHT GKLVLEIPPA 3551 LDPEGTVLVT GGTGALGQVV AEHLVREWGV RHLLLASRRG PEAPGSDELA 3601 SKLTGLGAEV TIVAADVSDP ASVVELVGKT DPSHPLTGVV HAAGVLEDGV 3651 VTAQTPEGLA RVWAAKAAAA ANLHEATREM RLGLFVVFSS AAATLGSPGQ 3701 ANYAAANAYC DALMQHRRAV GQVGLSVGWG LWEAPDAKPG VAADAKASAA 3751 TVGKASALSD GTNGSAPQDT TGTAPQGMTG GLTDTDVARM ARIGVKGMSN 3801 AHGLALFDAA HRHGRPHLVG FNLDLRTLAT HPLHTRPALL RGLATPTAGG 3851 ASRPTATAGG QPADLAGRLA ALSPSDRHHT LVRLIREQAA TVLGHHPDSL 3901 TTGSTFKELG FDSLTAVELR NRLSAATGLR LPAGLVFDHP DADILAEHLG 3951 AQLAPDGDTP AGAEATDPVL RDLAKLENAL SSTLVEHLDA DAVTARLEAL 4001 LSNWKAASAA PGSGSTKEQL QVATTDQVLD FIDKELGV* MonAV, polyketide synthase multi-enzyme MONS5, housing extension modules 7 and 8 Length: 4107 amino acids 1 MASEEELVDY LKRVAAELHD TRQRLREVED RRQEPVAVVG MACRFPGGIE 51 TPEGLWELVA AGDDAIEPFP TDRGWDLEGI YHPDPDHPGT CYVREGGFLA 101 APDRFDSDFF CPSPREALAS SPQLRLLLET SWEALERAGI NPASLKGSPT 151 GVYVGAATTG NQTQGDPGGK ATEGYAGTAP SVLSGRLSFT LGLEGPAVTV 201 ETACSSSLVA MHLAANALRQ GECDLALAGG VTVMSTPEVF TGFSRQRGLA 251 PDGRCKPFAA AADGTGWGEG AGLILLERLS DARRKGHKVL AVIRGSAINQ 301 DGASNGFTAP NGPSQRRVIR QALSSAHLST SEIDVVEAHG TGTRLGDPIE 351 AEALIATYGK EREDDRPLWL GSVKSNIGHT QAAAGVAGVI KMVMALQREL 401 LPATLNVDEP TPHVQWEGGG VRLLTEPVPW SRGERPRRAG ISSFGISGTN 451 AHVVLEEAPP EEDVPGPVAA EPEGVVPWVV SARTEEALSE QARRLGEFVA 501 DTDPSTADVG WSLTTSRAIL EHRAVVVGRD RDALTAGLAA LAAGEESADV 551 VAGVAGDVGP GPVLVFPGQG SQWVGMGAQL LDESPVFAAR IAECEQALSA 601 YVDWSLSAVL RGDGSELSRV EVVQPVLWAV MVSLAAVWAD YGVTPAAVIG 651 HSQGEMAAAC VAGALSLEDA ARVVAVRSDA LRQLMGQGDM ASLGASSEQA 701 AELIGDRPGV CIAAVNGPSS TVISGPPEHV AAVVADAEER GLRARVIDVG 751 YASHGPQIDQ LHDLLTDRLA DIRPATTDVA FYSTVTAERL TDTTALDTDY 801 WVTNLRQPVR FADTIDALLA DGYRLFIEAS AHPVLGLGME ETIEQADIPA 851 TVVPTLRRDH GDTTQLTRAA AHAFTAGATV DWRRWFPADP TPRTIDLPTY 901 AFQRRSYWLP VDGVGDVRSA GLRRVEHSLL PAALGLADGA LVLTGRLAAS 951 GGGGGWLADH AVAGTTLVPG AALVEWALRA ADEAGCPSLE ELTLQAPLVL 1001 PGSGGLQVQV VVGPADGQGG RREVRVFSRV DSDDEAAGQD EGWSCHATGV 1051 LSPEPGAVPD GLSGQWPPTG AEPLEISDLY EQAASAGYEY GPSPRGLRSV 1101 WRHGHNLLAE VELPEQAGAH DDFGIHPVLL DAALHPALLL DQNAPGEEQE 1151 PAQPALRLPF VWNGVSLWAT GAATVRVRLA PHGGGETDDS AGLRVTVADA 1201 TGAPVLSVDS LALRPADPEL LRTAGRAGSC TNGLFTVEWT ALPPADVADH 1251 AAGDGWAVLG QDVPDWAGAD MPRHPDMASL SAALDEGTQA PAAVFVETTA 1301 TSHATPNTAA DVTLDASGRA VAERTLHLLR DWLAEPRLAE TRLVLITHHA 1351 VTTPADDDVN AAPLDVPAAA LWGLIRSAQA EHPDRFVLLD TDAKANTDPG 1401 PDTSTDHSTA SGTYRTVIAR ALATGEPQLA VRAGELLAPR LAPAATPTPE 1451 TPTPETQPDT GSGSEAGAGS GSGPGATLDP DGTVTLIAGGT GMMGGLVAEH 1501 LVRAWSVRHL LLVSRQGPDA PDARDLADRL VGLGATVRIV AADLTDGRAT 1551 ADLVASVDPA HPLTGVIHAA GVLDDAVVTA QTSDQLARVW AAKASVAANL 1601 DAATSELPLG LFLMFSSAAG VLGNAGQAGY AAANAFVDAL VGRRRATGLP 1651 GLSIAWGLWA RGSAMTRHLD DADLARLRAG GVKPLLDEQC LALLDAARAT 1701 AAHTSLVVAA GIDVRGLNRD DVPAILRDLA GRTRRRAAAD STVDQAALER 1751 RLTGLDEAER RAVVTDVVRE CVAAVLGHRS AADVRTEANF KDLGFDSLTA 1801 VQLPNRLSAA SGLRLPATLA FDHPTPQALA AYLGTRLSGR TATPVAPVAP 1851 SAAATDEPVA IVAMACKYPG GATSPEGLWD LVAEGVDAVG AFPTGRGWDL 1901 ERLFHPDPDH PGTSYADEGA FLPDAGDFDA AFFGINPREA LAMDPQQRLL 1951 LEASWEVLER AGIDPTTLKG TPTGTYVGVM YHDYAAGLAQ DAQLEGYSML 2001 AGSGSVVSGR VAYTLGLEGP AVTVDTACSS SLVSIHLAAQ ALRQGECTLA 2051 LAGGVTVMAT PEVFTGFSRQ RGLAPDGRCK PFAAAADGTG WGEGVGVLLL 2101 ERLSDARRHG RRVLGVVRGS AVNQDGASNG LTAPNGPSQE RVIRQALASG 2151 GLSSVDVDVV EGHGTGTTLG DPIEAQALLA TYGQGRPVDR PLWLGSVKSN 2201 IGHTQAAAGV AGVIKMVMAM RHGVVPASLH VDVPSPHVEW DSGAVRLAVE 2251 SVPWPEVEGR PRRAGVSSFG ASGTNAHVIV ESVPDGLGED SVSVSGEAPE 2301 TETDGRLVPW VVSARSPQAL RDQALRLRDA VAADSTVSVQ DVGWSLLKTR 2351 ALFEQRAVVV GRERAELLSG LAVLAAGEEH PAVTRSREDG VAASGAVVWL 2401 FSGQGSQLVG MGAGLYERFP VFAAAFDEVC GLLEGPLGVE AGGLREVVFR 2451 GPRERLDHTM WAQAGLFALQ VGLARLWESV GVRPDVVLGH SIGEIAAAHV 2501 AGVFDLADAC RVVGARARLM GGLPEGGAMC AVQATPAELA ADVDDSGVSV 2551 AAVNTPDSTV ISGPSGEVDR IAGVWRERGR KTKALSVSHA FHSALMEPML 2601 AEFTEAIREV KFTRPKVSLI SNVSGLEAGE EIASPEYWAR HVRQTVLFQP 2651 GIAQVASTAG VFVELGPGPV LTTAAQHTLD DVTDRHGPEP VLVSSLAGER 2701 PEESAFVEAM ARLHTAGVAV DWSVLFAGDR VPGLVELPTY AFQRERFWLS 2751 GRSGGGDAAT LGLVAAGHPL LGAAVEFADR GGCLLTGRLS RSGVSWLADH 2801 VVAGAVLVPG AALVEWALRA GDEVGCVTVE ELMLQAPLVV PEASGLRVQV 2851 VVEEAGEDGR RGVQIYSRPD ADAVSGDDSW ICHATGTLTP QHTDAPNDGL 2901 AGAWPAAGAV PVDLAGFYER VADAGYAYGP GFQGLRAVWR HGQDLLAEVV 2951 LPEAAGAHDG YGIHPALLDA TLHPALLLDW PGEVQDDDGK VWLPFTWNQV 3001 SLRAAGAATV RVRLSPGEHD EAEREVQVLV ADATGTDVLS VGSVTLRPAD 3051 IRQLQAVPGH DDGLFSVDWT PLPLSRTDVS QTDADGDADW VVLSDGVGSL 3101 ADVVSAAGGE APWAVVAPVG ASAGGGLAGF DRREGLDGRL VVERVLSLVQ 3151 EFLAAPELAE SRLLVLTRGA VATGGDGDGD VDASAAAVWG LVRSAQSENP 3201 GRFILLDVDM DVDVDVDMDV DVDVDVDVDV DGDGNGSDLD PDLNGRRLPH 3251 ATLRHAAEEL DEPQLALRDG QLLVPRLVRA TGGGLVVAPT DRAWRLDKGS 3301 AETLESVAPV AYPGVMEPLG PGQVRLGIHA AGINFRDVLV SLGMVPGQVG 3351 LGGEGAGVVT ETGPDVTHLS VGDRVMGVLH GSFGPTAVAD TRMVAPVPQG 3401 WDMRQAAAMP VAYLTAWYGL VELAGLKAGE RVLIHAATGG VGMAAVQIAR 3451 HLGAEVFATA SAAKHVVLEE MGIDAAHRAS SRDLAFEDTF RQATDGRGMD 3501 VVLNSLTGEF IDASLRLLGD GGRFLEMGKT DVRTPEEVAA EYPGVTYTVY 3551 DLVTDAGPDR IAVMMSELGE RFASGALDPL PVRSWPLDKA REAFRFMSQA 3601 KHTGKLVLDV PAPLDPDGTV LITGGTGALG QVVAEHLVRE WGVRELLLAS 3651 RRGLDAPGSG ELADRLSDLG AEVTVAAADV SDPASVVELV GKTDPSHPLT 3701 GVVHAAGVLE DGIVTAQTPE GLARVWAAKA AAAANLHEAT REMRLGLFVV 3751 FSSAAATLGS PGQANYAAAN AYCDALMQRR RAAGQVGLSV GWGLWEAPDA 3801 KPGVAADAKP DVAADAKTGV AADGTPQGMT GTLSGTDVAR MARIGVKAMT 3851 SAHGLALLDA AHRHGRPHLV AVDLDTRVLA HKPAPALPAL LRAFAGDQGG 3901 QGGGRGGGRG GGPARPAAAT TRQNVDWAAK LSVLTAEEQH RTLLDLVRTH 3951 AAAVLGHAGT DAVRADAAFQ DLGFDSLTAV ELRNRLSAST GLRLPATFIF 4001 RHPTPSAIAD ELRAQLAPAG ADPAAPLFGE LDKLETVITG HAHDESTRTR 4051 LAARLQNLLW RLDDTSARSD HAAGASDADG DAVENRDLES ASDDELFELI 4101 DRELPS* MonAVI, polyketide synthase multi-enzyme MONS6, housing extension module 9 Length: 1701 amino acids 1 MPGTNDMPGT EDKLRHYLKR VTADLGQTRQ RLRDVEERQR EPIAIVAMAC 51 RYPGGVASPE QLWDLVASRG DAIEEFPADR GWDVAGLYHP DPDHPGTTYV 101 REAGFLRDAA RFDADFFGIN PREALAADPQ QRVLLEVSWE LFERAGIDPA 151 TLKDTLTGVY AGVSSQDHMS GSRVPPEVEG YATTGTLSSV ISGRIAYTFG 201 LEGPAVTLDT ACSASLVAIH LACQALRQGD CGIAVAGGVT VLSTPTAFVE 251 FSRQRGLAPD GRCKPFAEAA DGTGFSEGVG LILLERLSDA RRNGHQVLGV 301 VRGSAVNQDG ASNGLTAPND VAQERVIRQA LTNARVTPDA VDAVEAHGTG 351 TTLGDPIEGN ALLATYGKDR PADRPLWLGS VKSNIGHTQA AAGVAGVIKM 401 VMAMRHGELP ASLHIDRPTP HVDWEGGGVR LLTDPVPWPR ADRPRRAGVS 451 SFGISGTNAH LIVEQAPAPP DTADDAPEGA ATPGASDGLV VPWVVSARSP 501 QALRDQALRL RDFAGDASRA PLTDVGWSLL RSRALFEQRA VVAGRERAEL 551 LAGLAALAAG EEHPAVTRSR EEAAVAASGD VVWLFSGQGS QLVGMGAGLY 601 ERFPVFAAAP DEVCGLLEGE LGVGSGGLRE VVFWGPRERL DHTVWAQAGL 651 FALQVGLARL WESVGVRPDV VLGHSIGEIA AAHVAGVFDL ADACRVVGAR 701 ARLMGGLPEG GAMCAVQATP AELAADVDGS SVSVAAVNTP DSTVISGPSG 751 EVDRIAGVWR ERGRKTKALS VSHAFHSALM EPMLGEFTEA IRGVKFRQPS 801 IPLMSNVSGE RAGEEITSPE YWARHVRQTV LFQPGVAQVA AEARAFVELG 851 PGPVLTAAAQ HTLDHITEPE GPEPVVTASL HPDRPDDVAF AHAMADLHVA 901 GISVDWSAYF PDDPAPRTVD LPTYAFQGRR FWLADIAAPE AVSSTDGEEA 951 GFWAAVEGAD FQALCDTLHL KDDEHRAALE TVFPALSAWR RERRERSIVD 1001 AWRYRVDWRR VELPTPVPGA GTGPDADTGL GAWLIVAPTH GSGTWPQACA 1051 RALEEAGAPV RIVEAGPHAD RADMADLVQA WRASCADDTT QLGGVLSLLA 1101 LAEAPATSSD TTSHTSTSCG TGSLASHGLT GTLTLLHGLL DAGVEAPLWC 1151 ATRGAVSCGD ADPLVSPSQA PVWGLGRVAA LEHPELWGGL VDLPADPESL 1201 DASALYAVLR GDGGEDQVAL RRGAVLGRRL VPDATPDVAP GSSPDVSGGA 1251 AHADATSGEW QPHGAVLVTG GVGHLADQVV RWLAASGAEH VVLLDTGPAN 1301 SRGPGRNDDL AAEAAEHGTE LTVLRSLSEL TDVSVRPIRT VIHTSLPGEL 1351 APLAEVTPDA LGAAVSAAAR LSELPGIGSV ETVLFFSSVT ASLGSREHGA 1401 YAAANAYLDA LAQRAGADAA SPRTVSVGWG IWDLPDDGDV ARGAAGLSRR 1451 QGLPPLEPQL ALGALRAALD GGKGHTLVAD IEWERFAPLF TLARPTRLLD 1501 GIPAAQRVLD ASSESAEASE NASALRRELT ALPVRERTGA LLDLVRKQVA 1551 AVLRYEPGQD VAPEKAFKDL GFDSLVVVEL RNRLRAATGL RLPATLVYDY 1601 PTPRTLAAHL LDRVLPDGGA AELPVAAHLD DLEAALTDLP ADDPRRKGLV 1651 RRLQTLLWKQ PDAMGAAGPA DEEEQAAPED LSTASADDMF ALIDREWGTR 1701 * MonH, probable regulatory protein Length: 981 amino acids 1 VSGVERGVGS AGPVEQGDGL AGLVERAEAL AALRGAFDGS PGTGGSLVVL 51 SGAVGTGKTA LLRAWADRIG ADADALVLTA TACRAERDLP LGVLEQLVRS 101 PGLPPASAER ALAWWDEEAS ATPGKTDANG TSANGTDANG TGAGQTGAGQ 151 AGVGQTGVGG EPVLAASALR QLCEVLRDLL AERPVVVAVD DAHHADAASL 201 QCLLSVVRRL RSARLHVLFT EYAHQKAQNA LLSSEFLHEP ALRRIRLEPL 251 SKAGVEALLA RHLDERTAQD LTPVVHGMSA GHPLLVRALA EDHRAAGGAG 301 EAYGRAVLSF LYRHETPVTQ VARAIAALGA HAGPGQVGRL LDVDAASVER 351 AVRQLTVAEV LHEGRLCHPA FAAAVLDGMP PEERRALHGR VADLLHEEGA 401 PATEVAAHLV AADRSDAPWA VPVFQEAAQL ALDEDQVETG VDYLRAAHQR 451 CRGAAQRAAV VGALADAEWR LDPAKVLRHL PDPAAMAPQT DPAALAPHTD 501 PAPTAAPTAA PTPTPIPTTP PLPTHLLWHG RVEEGLDAIG TLTGPGPNPA 551 GAPPMNPADL DTPWLWGAYL YPGHVKERLG SGALSPQRST PPAVTPELQG 601 AGTLMNDLLH GGERDATEAA ERALNRYRLG PRTIAVQTAA LAALTYRDRP 651 HRAAAWCDGL VAQADERNSP TWRALFTAWR ALLHLRQGDP AAAEQRAETA 701 LALLGSKGWG AAIGLPLAAA VQAKAALGDV DGAAALLERP VPQAVFQTRT 751 GLHYLAARGR YHLATGCHYA ALCDFYACGT RMSSWGVDLP ALEPWRLGAA 801 EAYLALGEGL LARQLVDGQL PLPTPDDGRT WGMTLRLRAA TSPAPARAEL 851 LDEAVAVLRE SGDTFELARA VADQAVAVRE GGEAERARLL ARKAELLARR 901 WGSAPAPATV PEPPERPGPA TPDAELTSAE RRVAELAAEG FTNREISRKL 951 CVTVSTVEQH LTRIYRKLDV RRLDLQAALG * MonCI, flavin-dependent epoxidase Length: 496 amino acids 1 VTTTRPAHAV VLGASMAGTL AAHVLARHVD AVTVVERDAL PEEPQHRKGV 51 PQARHAHLLW SNGARLIEEM LPGTTDRLLA AGARRLGFPE DLVTLTGQGW 101 QHRFPATQFA LVASRPLLDL TVRQQALGAD NITVRQRTEA VELTGSGGGS 151 GGRVTGVVVR DLDSGRQEQL EADLVIDATG RGSRLKQWLA ALGVPALEED 201 VVDAGVAYAT RLFKAPPGAT THFPAVNIAA DDRVREPGRF GVVYPIEGGR 251 WLATLSCTRG AQLPTHEDEF IPFAENLNHP ILADLLRDAE PLTPVFGSRS 301 GANRRLYPER LEQWPDGLLV IGDSLTAFNP IYGHGMSSAA RCATTIDREF 351 ERSVQEGTGS ARAGTRALQK AIGAAVDDPW ILAATKDIDY VNCRVSATDP 401 RLIGVDTEQR LRFAEAITAA SIRSPKASEI VTDVMSLNAP QAELGSNRFL 451 MAMRADERLP ELTAPPFLPF ELAVVGLDAA TISPTPTPTP TAAVRS MonBII, carbon-carbon double bond isomerase Length: 141 amino acids 1 MPDEAARKQM AVDYAERINA GDIEGVLDLF TDDIVFEDPV GRPPMVGKDD 51 LRRHLELAVS CGTHEVPDPP MTSMDDRFVV TPTTVTVQRP RPMTFRIVGI 101 VELDEHGLGR RVQAFWGVTD VTMDDPAGPA DTTHPEGIRA * MonBI, carbon-carbon double bond isomerase Length: 144 amino acids 1 MNEFARKKRA LEHSRRINAG DLDAIIDLYA PDAVLEDPVG LPPVTGHDAL 51 RAHYEPLLAA HLREEAAEPV AGQDATHALI QISSVMDYLP VGPLYAERGW 101 LKAPDAPGTA RIHRTAMLVI RMDASGLIRH LKSYWGTSDL TVLG MonAVIII, polyketide synthase multi-enzyme MONS8, housing extension modules 11 and 12 Length: 3754 amino acids 1 MSNEEKLLDH LKWVTAELRQ ARQRLHDKES TEPVAIVGMA CRYPGGARSA 51 EDLWELVRDG GDAVAGFPDD RGWDLESLYH PDPEHPATSY VRDGAFLYDA 101 GHFDAEFFGI SPREATAMDP QQRLLLETAW EAIEHAGMNP HALKGSDTGV 151 FTGVSAHDYL TLISQTASDV EGYIGTGNLG SVVSGRISYT VGLEGPAVTV 201 DTACSSSLVA IHLASQALRQ GECSLALAGG STVMATPGSF TEFSRQRGLA 251 PDGRCKPFAA AADGTGWGEG AGVVALELLS EARRRGHKVL AVIRGSATNQ 301 DGTSNGLAAP NGPSQERVIR AALANARLSA EDIDAVEAHG TGTTLGDPIE 351 AQALIATYGQ GRPEDRPLWL GSVKSNIGHT QAAAGVAGVI KMVMAMRNGL 401 LPTSLHIDAP SPHVQWEQGS VRLLSEPVDW PAERTRRAGI SAFGISGTNA 451 HLILEEAPPE EDAPGPVAAE PGGVVPWVVS GRTPDALREQ ARRLGEFAAG 501 LADASVSEVG WSLATTRALF DQRAVVVGRD LAQAGASLEA LAAGEASADV 551 VAGVAGDVGP GPVLVFPGQG SQWVGMGAQL LDESPVFAAR IAECEQALSA 601 HVDWSLSDVL RGDGSELSRV EVVQPVLWAV MVSLAAVWAD YGITPAAVIG 651 HSQGEMAAAC VAGALSLEDA ARIVAVRSDA LRQLQGHGDM ASLSTGAEQA 701 AELIGDRPGV VVAAVNGPSS TVISGPPEHV AAVVADAEAQ GLRARVIDVR 751 YASHGPQIDQ LHDLLTDRLA DIQPTTTDVA FYSTVTAERL DDTTALDTAY 801 WVTNLRQPVR FADTIEALLA DGYRLFIEAS PHPVLNLGIQ ETIEQQAGAA 851 GTAVTIPTLR RDHGDTTQLT RAAAHAFTAG APVDWRRWFP ADPTPRTVDL 901 PTYAFQHKHY WVEPPAAVAA VGGGHDPVEA RVWQAIEDLD IDALAGSLEI 951 EGQAESVGAL ESALPVLSAW RRRHREQSTV DSWRYQVTWK HLPDVPAPEL 1001 SGAWLLLVPA AHADHPAVLA TAQTLTAHGG EVRRHVVDAR AMERTELAQE 1051 LRVLMDGAAF AGVVNLLALD EEPHPEHSAV PAGLAATTAL VQALADNGAD 1101 IAVRTLTQGA VSTSAGDALT HPVQAQVWGL GRVAALEYPR LWGGLVDLPA 1151 RIDHQTLARL AAALVPQDED QISIRPSGVH ARRLAHAPAN TVGSGLGWRP 1201 DGTTLITGGT GGIGAVLARW LARAGAPHLL LTSRRGPDAP GAQELAAELT 1251 ELGAAVTVTA CDVGDREQVR RLIDDVPAEH PLTAVIHAAG VPNYIGLGDV 1301 SGAELDEVLR PKALAAHHLH ELTRELPLSA FVMFSSGAGV WGSGQQGAYG 1351 AANHFLDALA EHRRAEGLPA TSIAWGPWAE AGMAADQAAL TFFSRFGLHP 1401 LSPELCVKAL QQALDAGETT LTVANFDWAQ FTSTFTAQRP SPLLADLPEN 1451 RRASAPAAQQ EDATEASSLQ QELTEAKPAQ QRQLLLQHVR SQAAATLGHS 1501 DVDAVPATKP FQELGFDSLT AVELRNRLNK STGLTLPTTV VPDHPTPDAL 1551 TDVLRAELSG DAAASADPVR AAGASRGAAD DEPIAIVGMA CRYPGDVRSA 1601 EELWDLVAAG KDAMGAFPDD RGWDLETLYD PDPESRGTSY VREGGFLYDA 1651 GDFDAGFFGI SPREAVAMDP QQRLLLETAW EAIERAGLDR ETLKGSDAGV 1701 FTGLTIFDYL ALVGEQPTEV EGYIGTGNLG CVASGRVSYV LGLEGPAMTI 1751 DTGCSSSLVA IHQAAHALRQ GECSLALAGG ATVMATPGSF VEFSLQRGLA 1801 KDGRCKPFAA AADGTGWAEG VGLVVLERLS EARRNGHNVL AVIRCSAINQ 1851 DGTSNGLTAP NGQAQQRVIR QALANARLSA EDVDAVEAHG TGTMLGDPIE 1901 ASALVATYGK ERPADRPLWL GSIKSNIGHA QASAGVAGVI KMVMALRNEQ 1951 LPASLHIDAP TPHVDWDGSG VRLLSEPVSW PRGERPRRAG VSAFGISGTN 2001 AHLILEQAPD APEPVTAPAE DAAAPAGVVP WVVSARGEEA LRAQARLLAD 2051 RATADPRLAS PLDVGWSLVK TRSVFENPAV VVGKDRQTLL AGLRSLAAGE 2101 PSPDVVEGAV QGASGAGPVL VFPGQGSQWV GMGAQLLDES PVFAARIAEC 2151 ERALSAHVDW SLSAVLRGDG SELSRVEVVQ PVLWAVMVSL ASVWADYGIT 2201 PAAVIGHSQG EMAAACVAGA LSLEDAARIV AVRSDALRQL MGQGDMASLG 2251 AGSEQVAELI GDRPGVCVAA VNGPSSTVIS GPPEHVAAVV ADAEARGLRA 2301 RVIDVGYASH GPQIDQLHDL LTERLADIRP TTTDVAFYST VTAERLDDTT 2351 TLDTDYWVTN LRQPVRFADT IEALLADGYR LFIEASPHPV LNLGMEETIE 2401 RADMPATVVP TLRRDHGDAA QLTRAAAQAF GAGAEVDWTG WFPAVPLPRV 2451 VDLPTYAFQR ERFWLEGRRG LAGDPAGLGL ASAGHPLLGA AVELADGGSH 2501 LLTGRISPRD QAWLAEHRVM DTVLLPGSAF VELALQAAVR AGCAELAELT 2551 LHTPLAFGDE GAGAVDVQVV VGSVAEDGRR PVTVHSRPTG EGEEAVWTRH 2601 AAGVVAPPGP DAGDASFGGT WPPPGATPVG EQDPYGELAS YGYDFGPGSQ 2651 GLVSAWRLGD DLFAEVALPE AESGRADRYQ VHPVLLDATL HALILDAVTS 2701 SADTDQVLLP FSWSGLRVHA PGAEKLRVRI ARTAPDQLAL TAVDGGGGGE 2751 PVLTLESLTV RPVAANQIAG ARAADRDALF RLVWMEVAAR AEETGGGAPR 2801 AAVLAPVESG PMGGTSAGAL ADALSDALAA GPVWDTFGAL RDGVAAGGEA 2851 PDVVLAVCAA PGAGAGAVAD ADGRGGDPAG YARLATVSLL SLLKEWVDDP 2901 AFAATRLVVV TRGAVAARPG ETAGDLAGAS LWGLVRSAQA ENPGRLTLLD 2951 VDGLESSPAT LTGVLASGEP ELALRDGRAY VPRLVRDDAS VRLVPPVGSL 3001 TWRLARCQEA GGGQQLSLVD APEAGRALEP HEVRVAVRAA APGPLTAGQV 3051 EGAGVVTEVG GEVGSVAVGD RVMGLFDAVG PVAVTDAALL MPVPAGWSWA 3101 QAAGSLGAYV SAYHVLADVV APRGGETLLV GEETGSVGRA VLRLALAGRW 3151 RVEAVDGAST ADDSGAERAA DVTLRHEGAL VVHRAGGRPD EGQAVVPPEP 3201 GRVREILAEL TELTELAEIT ESAEPGLPAE RGDSRALTPL DITVWDIRQA 3251 PAAMAAPPSA GTTVFSLPPA FDPEGTVLVT GGTGALGSLT ARHLVERYGA 3301 RHLLLSSRRG ADAPGALELA ADLSALGARV TFAACDPGDR DEAAALLAAV 3351 PSDHPLTAVF HCAGTVNDAV VQNLTAEQVE EVMRVKADAA WHLHELTRDA 3401 DLSAFVLYSS VAGLLGGPGQ CSYTAANAFL DALARHRHDG GAAATSLAWG 3451 YWELASGMSG RLTDADRARH ARAGVVGLGA DEGLALLDAA WAGGLPLYAP 3501 VRLDLARMRR QAQSHPAPAL LRDLVRGGSK SGGGAVSAGA AALLKSLGAM 3551 SDPEREEALL DLVCTHIAAV LGYDAATPVN ATQGLRELGF DSLTAVELRN 3601 RLSAATGLKL PATFVFDHPN PAELAAQLRQ ELAPRAADPL ADVLAEFERI 3651 EDSLLSVSSK DGSARAELAG RLRATLARLD APQDTAGEVA VATRTRIQDA 3701 SADEIFAFID RDLGRDGASG QGNGQPTGQG NGHGNGNGNG NGNGHGQAVE 3751 GQR* MonAVII, polyketide synthase multi-enzyme MONS7, housing extension module 10 Length: 1642 amino acids 1 MAHTEEKLLE YLKRVTADLR QTERRLQDVE SAGHEPVAVI GMACRLPGGV 51 RSPEEFWELV STGGDAVAPL PGNRNWDLDS LYDPDPESTG TSYVREGGFV 101 YDAGDFDPTF FGIGPTEAAA MAPQQRLALE TAWEAIERAG IDPLSLRSSD 151 TSTFIGCDGL DYALGASEVP EGTAGYFTIG NSGSVTSGRV AYTLGLEGPA 201 VTVDTACSSS LVSLHLATQA LRTQECSLAL AGGTYVMSSP APLIGFSELR 251 GLAPDGRCKP FSASSDGMGM AEGTGVVLLE RLSDARRKGH KVLAVIRGSA 301 INQDGASNGL TAPNGPAQER VIRAALANAR LAPEDIDAVE AHGTGTTLGD 351 PIEAGALISA YGRERPEDRP LWVGAVKSNI GHTQIAAGVA GVIKMVLALR 401 HDLLPAILHV DAPSPHVEWD GSGLRLLTDP VKWPRGERPR RAGVSSFGFS 451 GTNAHLILEE APPEEEDVPG SVAEEPGGVV PWVVSGRTPD ALRAQARRLG 501 EFAAGPADAS AADVGWSLTT TRSVFEHRAV VVGRDRDALT AGLGALAAGE 551 ASAGVVAGVA GDVGPGPVLV FPGQGSQWVG MGAQLLDESP VFAARIAECE 601 RALSAYVDWS LSAVLRGDGS ELSRVEVVQP VLWAVMVSLA AVWADYGVTP 651 AAVIGHSQGE MAAACVAGAL SLEDAARIVA VRSDALRRLQ GHGDMASLST 701 GAEQAAELIG DRPGVVVAAV NGPSSTVISG PPEHVAAVVA DAEARGLRAR 751 VIDVGYASHG PQIDQLHDLL TERLADIRPA NTDVAFYSTV TAERLTDTTA 801 LDTDYWVTNL RQPVRFADTI EALLADGYRL FIEASAHPVL GLGMEETIEQ 851 ADIPATVVPT LRRDHGDTTQ LTRAAAHAFT AGAPVDWRRW FPADPTPRTV 901 DLPTYAFQHQ HYWLERSASA SGAVSGEQSA AEAQLWHAVE ELDLGLLAET 951 LGSEEGSEEA VRALEPALPV LKGWRRRHQD QATIDSWRYR VTWKQRSDGP 1001 APELGGDWLL FVPADKAEHP AVRATAEALS EHGAAAVRLH PVETGRAGRQ 1051 ELAAVDTAGL AGIVNLLALD EEPHPEHPAV PAGLAATTAL LQALGDNGTT 1101 APLHTVTQGA VSTGATDPLT HPLQAHVWGL GRVAALEHPR LWAGLVDLPA 1151 RIDRHTLPRL AAALLPQDDE DQTAVRPTGI HHRRLTHAVG SIQNPVHSEA 1201 TWRPRGTTLI TGGTGGIGAV LARWLARQGA PRLHLTSRRG PDAPGARELA 1251 AELDGLGTAV TITACDVSDP RQLSGLIDDM PAEHPLTAVI HAAGMTDLTA 1301 IGDLTTARLG EVLGSKSDAA WNLHELTRDL DLSAFVMFSS GAGVWGSGQQ 1351 GAYGAANHFL DALAEHRRAQ GLPATSIAWG PWAEAGMSAD PESLTYFKRF 1401 GLLPIAPDLC VKALHQAVDA GDATLTVANF DWAKFTPTFT AQRPSPFLDD 1451 LPENQREAEQ TGTAAETSAF REELAKTPAS QRLGFLVQQV RTYAAATLGR 1501 TVEDIPAAKP FQELGFDSLT AVQLRNQLNT TTGLSLPATV IFDHPTPEAL 1551 ATHLRGQLGD GAEVAGEGDV LAALDKWDTA FGAAEVDEAA RRRIVGRLQV 1601 LVSKWSPAQD GPEGTDSAHA DLEAASADDI FDLISSEFGK S* MonD, cytochrome P450 hydroxylase Length: 431 amino acids 1 VGLTVGPDNA KRGIVPITDS KPAATFPDLV DPSFWARPHA ERVALFEEMR 51 GLPRPAFIRQ NMPGVPWTFG YHALVKYADI VEVSRRPQDF SSNGATTIIG 101 LPPELDEYYG SMINMDNPEH SRLRRIVSRS FGRNMIPEFE AVATRTARRI 151 IDELIARGPG DFIRPVAAEM PIAVLSDMMG IPAEDHDFLF DRSNTIVGPL 201 DPDYVPDRAD SERAVIEASR ELGDYIAGLR AERLAAPGND LITKLVQVQA 251 DGEQLTRQEL VSFFILLVIA GMETTRNAIS HALVLLTEHP EQKQLLLSDF 301 DTHAPNAVEE ILRVSTPINW MRRVATRDCD NNGHRFRRGD RIFLFYWSGN 351 RDESVFPDPY RFDITRGTNA HVTFGAVGPH VCLGAHLARM EITVLYRELL 401 AALPQIHAVG QPRRLDSSFI EGIKHLHCAF * MonRI, probable activator protein Length: 268 amino acids 1 VRYEMLGPLR IKDGNDYATI NAQKVEIVLT VLLIRADRVV SLEQLMREIW 51 GEDLPRRATA GLHVYISQLR KFLKVPGSAG NPVETRAPGY VLHKRDDDQI 101 DAQIFPELVD VGRSLLREKR PDEAASCFGQ ALALWRGPIL GQGGNGPGTN 151 GPIIDGFSTW LTEIRLECQE MLVECQLQLG RHREAVGMLY ALTAENPMCE 201 AFYRQLMLAL YRSERQADAL KVYQSVRKTL NDELGLEPGR PLQELQRAIL 251 AGDMHLMSPP PLALSGR* MonAX, thioesterase Length: 278 amino acids 1 LSAFLAKGKI LSAFPPPDMS DPWIRRFRPR PEAVVRLVCF PHAGGSASYY 51 HPLAQSPTLP TDSEVLAVQY PGRQDRRRER LLDDIGELAD LITDALGPFD 101 DRPLAFFGHS MGAVLAYEVA QRLRERTGKQ PCRLFVSGRR APSRFRRGTV 151 HLLDDTELAA ELRRAGGTDP RFLDDEELLA EIIPVVRNDY RAVELYRWNP 201 SPPLSCPITA LVGDRDPQAP LDEVEAWQQH TEGPFDLKVF AGGHFYLNTN 251 QQGVTEVISK ALADSAQQRA TARGNAR* ORF29, a homologue of CapK involved in cell wall biosynthesis Length: 428 amino acids 1 LADLVAHARS ASPYYRELYH GLPERIEDPT LLPVTDKKQL MDHFDDWPTD 51 RDITFEKVRA FTDDPELIGR RFLGRYLVAT TSGTSGRRGL FVLDDRYMNV 101 SSAVSSRVLA SWLGPLGIAR AVVHGGRFAQ LVATEGHYVG FAGYSRLRQD 151 GEARSKLVRA FSVHEPMSRL VAELNEYRPA FVIGYASTIM LFTAEQEAGR 201 LHIDPVLVEP AGETMTESDT DRIAAAFGAK VRTMYSATEC TYLSHGCAEG 251 WYHVNDDWAV LEPVDADHRP TPPGEFSHTT LISNLANRVQ PFLRYDLGDS 301 VMLRPDPCPC GTPSPAIRVQ GRSGDILTFP SGRGDDVSLA PLAFSSLFDR 351 MPGVELFQIE QTAPSTLRVR VVQAPGADAD HVWQRAHDGL THLLADNKLD 401 NVTVERGEEP PRQASGGKYR TIIPLAA* LipB, lipase B Length: 338 amino acids 1 VKVPVEVTVR LSSWLGGLVA AVLAATVLPA SAASAADVSS PPLEIPAAEL 51 AKALHCGTEL GDLRDAGDKP TVLFVPGTGL KGEENYAWNY MAELKKKGYQ 101 SCWVDSPGRG LRDMQESVEY VVYATRAIQE ATGRKVDLVG HSQGGLLTAW 151 ALRFWPDLPG KVDDMVTLGS PFQGTRLASP CRPIAEVAGC PASVLQFARD 201 SMWSKALGAD GTPMPAGPSY TTIYSYADES VVADGEAPSL PGAHRIGVQD 251 ICPGRPWPTH IAMVVDQVSY DLVADAIEHP GPADTSRIDR AHCAKPVMPL 301 NSQEAVDALP GLLNFPIELL THSQPWVDEE PPLRPYAR ORF31, putative ion pump Length: 309 amino acids 1 MGHDHGPSAG AAGGTLSGTY RKRLLWTIGI SGSITVIQVV GALLSGSLAL 51 LADAAHSLTD AVGVSLALGA ITLAQRAPTP RRTFGFCRVE IFSAVLNALL 101 LVVIFAWVLW SAIGRFSEPV EVKGGLMFVV ALGGLAANLV GLWLLRDAKE 151 KSLNLRGAYL EVLGDALGSV AVIVGGLVIL LTGWQAADPI ASIVTGLLIV 201 PRAYGLLRDS LHVLLEATPQ DVDLGEVRRH LLEERGVVAV HDLHGWTVTS 251 GMPVLTAHVV VTEEALASGY GELLGRLQRC VGGHFDVAHS TIQLEPEGHV 301 EEDGALHT* ORF32, hypothetical membrane protein Length: 364 amino acids 1 MTRALTLHDW IVAGIAVVAG VVAGLLLRAL LRWLGERASK TRWSGDDVIV 51 DALRTLVPCA AITAGLAAAA GALPLTPRTG RNVTMTLTAL LILAATLTAA 101 RIVTGLVKAV AQSRSGVAGS ATIFVNITRV VVLAMGFLIV LQTLGISIAP 151 LLTALGVGGL AVALALQDTL ANLFAGVHIL AAKTVQPGDY IQLSSGEEGY 201 VVDINWRNTT VRQLSNNLVI IPNAKLAGTN MTNYSRPEQE LSIMVQVGVS 251 YDSDLEQVEK VTTEVVDEVM AEITGAVPDH EAAIRFHTFG DSRISFTVIL 301 GVGEFSDQYR IKHEFIKRLH QRYRAEGIRV PAPVRTVRVQ QGELPPPLGI 351 PHQRDTSTQA RLH* AmtA, glycine amidinotransferase (partial coding sequence) Length: 131 amino acids 1 MSPVNSHNEW DPLEEIIVGR LEGATIPSSH PVVACNIPTW AARLQGLAAG 51 FEYPQRLIEP AQQELDQFIA LLQSLDVTVR RPAAVDHKHR FGTPDWQSRG 101 FCNSCPRDSM LVVGDEIIET PMAWPCRCFE T

[0153]

1 52 1 30000 DNA Streptomyces cinnamonensis Nucleotides 1 to 30000 of the monensin biosynthetic gene cluster 1 gatcagcgcg gtggcgtcgt cggcgtccag ctcgttctgc gtggcggacg gcagcgcgat 60 gtcggcaggc acctcccaga cccggcggcc cggcacgaag cgggccgagg cgccgcggcg 120 ctgggcgtag gtgtccacgc gggcgcgttc gacctccttg acctgcttga ggaggtccag 180 gtcgatgccc ttctcgtcga cgacgtaacc ggaggagtcc gaacacgtca cggcgttggc 240 gcccagggcg gcgagcttct ggatggtgta gatggcgacg ttcccggagc cggacacgac 300 cgccgtccgg ccttcgaggg tctcgccgcg ctcacgcagc atcgccgccg cgaagaggac 360 gttgccgtag ccggtcgcct ccggacggat cagggagccg ccccagttgc ggcccttgcc 420 ggtgaggacg cccgcctccc agcggttggt gatgcgccgg tactgaccga acagatagcc 480 gatctcccgg ccgccgacgc cgatgtcgcc cgcgggcacg tccgtgtgtt cgccgatgtg 540 ccggtacagc tccgtcatga acgactggca gaaacgcatg acttccgcgt cgctgcggcc 600 gcgcgggtcg aagtcgctgc cgcccttgcc gccgccgatg ccgaggcccg tcagcgcgtt 660 cttgaagatc tgctcgaagc ccaggaactt gatgacgccg aggttcaccg acgggtggaa 720 gcgcaggccg cccttgtacg ggccgagggc gctgttgaac tccacccgga agccgcggtt 780 gacccgcacg cgaccgtggt cgtcctgcca cggcacccgg aagacgatct ggcgctccgg 840 ttcgcacagg cgctcgatca ggccggcttc ggcgtactcg gggcgagccg cgatgaccgg 900 cgccagggtc tcgaggacct cgcgggcggc ctggtggaac tccggctggg ccgggttgcg 960 gtgttcgatc tcggtgagca gctgggagag tgctgtcttc tgcgagagag ctgtcttcgt 1020 gtcgggtcgc gtggtcaaag gagccctttc tggcacggcc ggcgtaggcg ctcggcgccg 1080 ttgccgtgcg cagggagacg ctcgagccgc aagtatgacg cgcatgtaaa cacagcgacc 1140 agccccccgg tccagggagt gaccaccatg cgagaccggg ccaccggtag ggccaccggt 1200 ccggcctgcg gaccccgtgt cacttccggc tcgcggccag gggtgccgcc cggcggaccg 1260 aatcggcgga ggcggccagc agtggcatgc ggacggccgg gctgggaatg cggttctggg 1320 cgtgcagcac tcccttgatc accgtcgggt tcggttcggt gaagagggcg gcggaaaggc 1380 gggcgaggtc ggctccgaga gcgcgggcgg gtgcggcgga gccgcgtcgc cacagcgcga 1440 tcatctcggc gtagtcggcg gtacgcagat tggccgacgc cacgattccg ccgtgggcgc 1500 ccgcagcgac cagcggcgag aggacgatgt cgtcaccgcc gagcacggcg aagccgggca 1560 ggggcgagtc gagcaactcc atggtggtcg ggtcgatcga gccggtcgcg tgcttgatgc 1620 cgacgacctc cggcaggcgg ccgagtgcgg tgatcgtgcc cgcgccgagc gtctgcccgg 1680 tgcggtaagg gatgtcgtac acgaccaggg ggaggccgcc gtgctcggcc agcgcggcga 1740 aatgagccag ggtccccgct tccccggggc ggatgtaggg cggcgcgggg accagcgcgg 1800 cggcgacgtc accccgggcc gccagctctc gcagggccgt gatggcggtg gcggtgtcgt 1860 tggtgcccac cccgacgatg agcggtgccc cgtgtgcccg gcacgcggcc gagcagacgc 1920 ggatcaccgt ctctctctcc tcggcggtca gtgtggcggc ctcggcggtc gtaccgaggg 1980 cgacgagccc ggaggcgccg gccgacagcg cctcgtcggc gagtcgggcc agcgcctcgg 2040 gggccaggcg cagatcgtcg gtgaacggag ttaccagggg gacgtacagg ccgttgaaga 2100 gcggttcggt ggtcggttcg aggctcgatg cgagggtcat gctcttaccc tggcccacgc 2160 cactcggtag atccatttca gattcctgcc gtcacaccta agctgaactt atgctcgatg 2220 tccgtcgcct ccatctgctc cgcgaactcg accggcgggg caccatcgcc gccgtggccg 2280 aagcgctgac cttcaccgcg tccgccgtct cccagcagct cggcgtgctg gagagggagg 2340 cgggcgtgcc gctgttggaa cgcagcggca ggcgcgtggt cctcacgccc gcaggacgct 2400 ccctcgtcgc acacgccgac gcggtgctga accgtctcga acaggcggtc gccgagctgg 2460 cgggcgcacg ggacggcatc ggcgggccgc tgcgcatcgg gacgttccct tccggcggcc 2520 acaccatcgt ccccggcgcg ctggccgaac tggcctctcg tcaccccgcg ttggagccga 2580 tggtgcggga gatcgactcc gcgcgcgtct ccgacggtct gcgggccggt gagctggacg 2640 tggccctcgt acacgactac gacttcgtac ccgcgacgcc ggacacgacc gtggacgagg 2700 tgcctctgct cgaagagccg atgtacctcg tcacccatgc cgcggacact gccacggact 2760 ccggctccgg gagcacactg gcagcgctgc tcgggccctg tgccgaggtt ccgtggatca 2820 cggcgcggga cggcacgacc ggtcacgcga tggctgtacg cgcctgtcag gccgccgggt 2880 tccagcccag gatccgccac caggtcaacg acttccgcac ggtgctggct ctggtcgccg 2940 ccgggcaggg ggccgggttc gtgccgcgga tggccgccga gccgagcccc gcgggcgtgg 3000 tgctcacgaa gctgccgctg ttccgtcgct cgaaggtcgc gttccgtgcg ggcggcggtg 3060 cccatccggc gatcgccgct ttcgtggccg cggcgacgac ggcggtcgaa cgcatggcgg 3120 gttcacgagg cccggccggc ggctctgagt gaaccggccg accgtgggaa tgtgtgtgcc 3180 ctgggccgca ccattcgtgg cctggtgacg tcctggcgac gtcctgacgt cctgatgtcc 3240 gaacgagaag gcgattttcc gcgatggccg atgacgcgta cctgttcctc ctccccgacc 3300 ggcacccccg actgggagcg gccctcgccg ccgtcggtgc cttggaatgc acggaaaccc 3360 ctgcggtgca cgcctggttg caggctcatg aggcctccgt gtcctcggaa caggtcagga 3420 ttctgcccgc cgatgccgag acactcatcc cgaaggacgc cgagcggctg ccggtgccgt 3480 tgagcgagga ggaggcgctc aaggtcgagc aggagtgcgc gccccagacc gtcacggaca 3540 tggagagcga actgctcgcg ttccgggaga cgacccagga ctggcaggcc ctcgtgcacc 3600 gggccctgac cgcgggcatc cccgcgcagc gcatcgcccg gctgaccgga ctcgacccgg 3660 aggagatcgg ccgcctgtag gcgctagcgg ccgcccagtg cggacaccag gatggcgacc 3720 gtgacggtgt tgaagacgaa ggcgatgacc gtgttcgccg ccacggtccg tcgcatgtcg 3780 cgtgaggtga cgtcgacatc ggtggtgccg aacgtcgtca tcgcggccag ggcgaaatag 3840 acgtagtcgg cccaggcggg actccgctcc ccggggaatt ccagtgcccg ctcgttctcc 3900 acgaggttgt cggcctggaa ggtgacggcg aaggccacga ccacgcagat ccaggcggcg 3960 acgaccaggg cgagcgccac cagggtgcgg gggagcgcgg agaaggtggt gctgaggtgg 4020 ccgggaagcc acagcaccgc caccaccagc gcggcagccg cgatgaagag cgaacccccg 4080 gggccgggcg cggttccgag gacgtaacgc tgcaggaatg tgccgcgggc ttcgcgccgc 4140 gcccaggagc ggacctgctc cggagcgacg ctcacgaaga cggtcatggt gatggcgagg 4200 tagggcagca ggtaggcgaa gaagacgagc acgccgacat ccgctgccga aatccgcacc 4260 acggcgtcga tggggaggac cactgccgcg cacgccgcga cggccaggct caccgccgac 4320 cggcgccgtt cggaaagcca gcgatgcacg gacgagcctc tctggtcggg cgtcgggcct 4380 cgtgtgatcg tgaccggctc cgcgcccgcc gaaagcgcgg tgcgatctcc tgccctcgaa 4440 cgagcgaaac gcttgcgccg gaaagcctcc ctgctgatgc cgacggcggc ggcagtggct 4500 gcggatgcgg atcgtgcgct gtgccctgac cctggatggg gggaggaacg cagagaggca 4560 ggtgcgccca tgacggtcat ggacaagctc aagcagatgc tcaaggggca cgaggacaag 4620 gccggccagg gaatcgacaa ggcgggcgac ttcgtcgacg ggaagacgca gggcaagtac 4680 agcggtcaag tcgacacggc ccaggacaag ctccgggacc agttcggctc ggatcagcag 4740 gagcctccgc agaggtaggc agcgtcaggg cggaatcggt ccgggcgacc gctgaccgct 4800 gatgcagatg ccgcagacgt cggccccgca ctcctccggg taaatcggag cgtaggcggg 4860 gccgacgtgt gcgcgtgcgg cctcgtctct gccgcccctc tccgccccgt ctctggcccc 4920 ttggtgccag tctgacggga aaatggcacc acttggtgcc acgcatgtgc catgatggcg 4980 tcatcgagag cgcgctgccc cgactcgcgg gcaggaaggg cgcgttccgc ggagtcggcc 5040 gtcggagggg ttgcatcatg gggacagcac agagccagga gcaggccgcc gcgcccggtg 5100 cctgcgccgc cttcgtccgc ttcgtgctct gcggtggcgg agtgggcctc gcctccagct 5160 tcgccgtggt cgccctcgcc tcctgggttc cctgggcgct ggccaacgcc ctggtcgccg 5220 tggtctccac cgtcgtcgcc accgagctcc acgcccgctt caccttcggt gcgggcgggc 5280 gcgcgacctg gcggcagcac gcgcagtcgg ccgggtccgc ggcggccgcg tacgcggtga 5340 cctgcgtggc gatgttcgtc ctgcagcagc tggtggcggc gcccggcgcg gtgctcgagc 5400 aggtcgtgta cctgtcggcc tccgcgctcg ccggtgtcgc gcggttcgtg gtgctgcgcc 5460 tcgtcgtctt cgcccggaac cgctcgctgc ccgccgcggc cgccgtgcgc accgcgcgtc 5520 ccgtgcgtcg cgtgccggcg cccgtgcccg cgaccgtggc ccacgccgca tcgcgcccgg 5580 ccggccccgc ggcgctctgc cccgccgcat gactccgtgc ccgcatgttt gtgcccccgg 5640 tgctccgtgc gtccgggggc ggggtgggcg tcgtgcccgg gtggtccagg ggtcacgcgg 5700 tggtgtgtgc cagttcctgg ccgaggtggt gggcgagctg tgcgggcgtg gggttctcga 5760 cgatggcgac catcgcgatc tccatcccgg tcagcgtcat cagtgtcttg gtgagctcaa 5820 gggcggtgag ggagttgaga ccgttctcga ggaagttgct gtcgtcgctg agggtggtgt 5880 tcagaagggt gccggcctgg gtgcggatgg tgtcggtgag gagcttctcg cgctcctcgg 5940 gggtggccgc ggcgagctgc ttctccagct cggtggcgtc ctggccggag gtgtggtcgg 6000 tgctggtcat gactgctcct gtgtgagtga ggtgttggcg ggggtcacac cgcggcgtgc 6060 gcggtgtggt cgtgcagcca gtaacgcgtg gcctggaagg agtacgtcgg gaggtcgatg 6120 gtccgggggt ggggggtgcg ccggacgaga ggggtccagt cgacggtgcc gcccgtggtg 6180 tgaagccgcg cgagggcggt caacagggcg cttacggcgg aggtttgcgt gccttccggt 6240 gagagcgcgc ccaggtggag aagcgtgtgg gtctcggggg tggggggtgc ggtgggggcc 6300 ggcgaggtga ggtggtggtg ccagtagtcg gcggaggcga tgggggtgtc ggccggggca 6360 gtgctggtga gcgtgagcgt ggcgcgttgg aacgtcagct gcttcagcac gggctcgtag 6420 gcgtcgggcg gagccggttg ttcaccctcg gcggcctggg cggcagcggc gtgggcggcg 6480 gccaggcggc acgcgtcgtc gagggtcagg attcccgcgg cgtacgcggc ggcgatgtgg 6540 ccgacaccgt cgccggtgag ggtgtggggg cgtacccccg tttccaggag cagccgcgcg 6600 agcgcggtgt ggaccgcgaa gcgcgccagt tcggagtggg gagtggggag gggagtcggc 6660 agatgggtgt cgaggagcgc gcgcgcttcg tcgaaggcgg acgcgaagag cgggaacgcc 6720 gagtggaact cggcacctcc gaaagccgcg ccgaatgtag cgccgaatgt cgcgccgggt 6780 ttggctccgg gtgccgcccc cgtcgtcacc ccgtcggccg ggcggccgtc gaagtgccag 6840 gcgatcttct tcgggccggc cccgggcgtg gacctgacca ggtccgggtg gtcctctccg 6900 gcggccaggg cgcgggcggc ggcgaggagt tcggtgtggt cggtgccggt gaggacggcg 6960 cggtgttcca gggggctgcg ggtggcggcg agcgagtagg cgacctcggc gggggagggc 7020 gcggggtcgg tggccgccag gtgggtgacg agggccttcg cctgtgcccg cagggcctcg 7080 ggtgtacgag cggacaggct ccaggccacc gggagttccg gggcaacggg cgacgtctgg 7140 tcgcgggcgg catccggcac cggagcctcg tccaccggcg gctcttcgag gatgaggtgc 7200 gcgttcgtgc cggacgtggc gaaggcggag atgccgaccc ggcggggctc ctcgcggcgg 7260 ggccagtcga ccgcctcggt gagcagccgt accgcgccct tcttccaggc ggcgaggggc 7320 gtcgggcggt cgacgtggag ggtcggcggc agggtgccgt gccggaacgc ctggaccatc 7380 ttgatgagcg cggccgcacc cgcggccccc tgcgtgtgcc ccgtgttgga cttgacggag 7440 ccgagccaca ggggccggtc gggggagcgg tcggcgccgt aggtggcgag gagggcctgg 7500 acctcgatgg cgtcgccgat gggggtgccc gtcccgtgcg cctcgacggc gtcgatctgg 7560 tccggggtga gcccggcgtc ggcgagggcg gcgcggatca catgctgctg ggaggggccg 7620 ttgggggcgg cgaggccgta tccggcgccg tcctggttga ccgcggagcc gcggatgacg 7680 gcgagcaccg ggtggccgtt cttcctggcg tcgccgagcc gctcaagcag gacgaggccg 7740 acgccttcac cgaggcccat gccgtcggcc gcggcggcga acggtttgca acggccgtcc 7800 tgcgcgagcg acttctggtg ggcgaaggcg tggaaggtgt gcggcgtcga catgacggtg 7860 ccgccgccgg cgagggcgag gccgcactcc ccgcggcgca gcgcctggca ggccaggtgg 7920 agggcgacca gggaggacga gcaggccgtg tccacgctga tggcggggcc ctcgaggccg 7980 agggcgtagg cgatgcggcc ggagacgagg ctgccggacg tgccgccgcc cagatagggc 8040 agcagctcgt cgggcgcggt ctcgagccgt gtcgcgtagt cgtgcccggt ggcgccgacg 8100 tagacgccgg tgagggtgga gcgcagggtg tgcggggcga tgtggccgcg ttcgacggtc 8160 tcccacgcga ggtggagcat gaggcgctgg aggggttcgg tggccacggc ctcggtgtcg 8220 ctgatgtcga agaagcccgc gtcgaagccg gccgcgtcgt ccaggaaccc gccgagctcc 8280 gcgtacgggc gttcctcggg gagttcccag gcgcggtcgt cggggaagcc ggtgacggcg 8340 tcgcggccct cggacaccag atcccacagg tcgtccgggg tgcgggtctt gccgggcagc 8400 cggcaggcca tggagacgac ggcgatcggc tcgtgctgtg cggccttcag ttcgcgcagc 8460 tgctgctggg cctggtggag ctcggccgtc gtccacttga ggtattcgac gagcttctct 8520 tcgttcgcca cgggaatggt cagccttcct gttctcgcgc gtgaagcctc aggtgggacg 8580 aggtcgggca aggtgggcag gcaggagccg cgcgctgtgg gtgccagggt cgccgcggct 8640 gcttaagcgg gtctaactcc cgccttgccg ccgggcatcg cctcgcacga gcgggccagc 8700 agcaggaggt cggcggcgat ctcgtcgggt gcgccggcgt gcagatcgtg gtcggagccc 8760 gggtaccagc gcacgctcac ctgctccagg gccgcctcgg cggcggccac ccaggcccgt 8820 acctggtcgg acagttgggg gatggcgggg atgaggggca gcagccgcac cggcacggtg 8880 accttgggat accagtcggc cggtgcctcc cgttgcaggc cggcgacgat cgacatgacc 8940 tgtgtcgagg tcaggcgggg gatgagcagg ccgtccggcc cgacgcggta gtccgccagg 9000 cgtgcctcga tggacgtggg cgaccagtcg ggatgggtgg cccgcaggta ggcgcgcatg 9060 tcggcggcgc tggtggtgcc ctgctgggcg cgccggacca cgtcggcggt gcgctcccag 9120 aaggcgcgca tcaccggtcc gtcgaactcg taccagccgc cgtcgatcag ggcgagaccg 9180 gccaccaggt ccgggtgctc ggccgccagg cgcagcgcga ggtgcgcgcc ccaggagtgc 9240 ccggccacca gtgcgccgga caggtcgagg gcggtgacgg ccgccaccag gtcggtgacg 9300 accgtcgcgt tgtcgtaccc gtcgggcggg gtgtccgact cgccgtggcc gcggtggtcg 9360 acggcgtagg ccgggtgtcc ggcggcggcg agacgggcgg cgacctcgtc ccacatccgg 9420 gcgttcgaca gcatgccgtg cagcagcagg aacggacggc ccggggctcc cggcccgtcc 9480 gcgggccggt acctgacatt gagggagacg gtctgcgaca cggggatgcg gaggttcttc 9540 acaggcgggc ccttgtgatc ccttgtgctg ggggaggaaa gcgggggcgg cacgctcagg 9600 ggcgctgcgc ggtcgcgaag atgtatccga gctcgggcat cttgccgagg gccgcctggt 9660 tgtgcaggaa cagctcgtat ccctctacgc cgatgatgtc gacgtactcg tcccggtggg 9720 cgcggatcca ctcgacgtaa ccgtcgtagg tcttggcggt ctcgcgggtg atgtcggtca 9780 gttcgaggac ggtccagccg gcggcgcgga agatgtcggg gtagtccccg atgtcggtga 9840 gcgcggcgta gatcgtggtg tcgctgacgg tggcggtccg gggccggctg ggatcggggt 9900 tgaggtagac catgtcggcg atcggcatcc gcgcgccggg cttcacgacg cggtgggcct 9960 cggtgagcac ctgctgcttg tccggcatgt gcagcatgga ctccagggcc cagcagtggt 10020 cgaaggagcc gtcgtcgaac ggcaggttca tggcgtcgac ctgctcgaag cggacccggt 10080 cggcgaggcc ggcctcgcgc gcccggcggt tgccgcgctc gacctggcgg gcgctgacgg 10140 agatgccgac cacctcgacg tcgcgggcgc gggccagctg catggccggg gtgccgttgc 10200 cgcagccgat gtcgaggacg cggtcgccgg gggccgggtc gaggcggcgg atcatctcgt 10260 cggtcatctg gaccatggcc tcgtcgaacg tggcctgctg ctcgccgccg tcgaaccagt 10320 agccgtagtg cagattgccg tctccgagct gagtcatcag gtcgaagacc ttgtggtcgt 10380 agtagtggcc gatgtcgctg ggctcggggg cgacggtctt gttcaccgtc gggggcttct 10440 tggtcgtcgc gttcttcgtc acggcttcag cgtcaccgtg cggcggcagg cgccacaacc 10500 ccacccccgc ccctcaaaag cccctatggg ccctcctcga ccgcccctag ggagctgctc 10560 ttgacgcgtt ccatacggaa cgggtggtac ccctccgaaa aaaatgagag tacgctccca 10620 ctagatattg agctctcttt aggaggtcga ctcccatgtc tgctgatctg ggtgcgcggc 10680 ggtggtgggc cgtcggtgct ctcgtactcg cctcgatggt cgtgggcttc gatgtgacga 10740 tcctgagcct ggcgttgccc gccatggccg acgacctcgg cgcgaacaac gtcgagctgc 10800 agtggttcgt gacgtcgtac acgctggtgt tcgcggccgg catgatcccg gccggcatgc 10860 tcggtgaccg gttcggacgc aagaaggtcc tgctcaccgc cctggtgatc ttcggtatcg 10920 cctcgctggc ctgtgcctac gcgacgtcct ccggcacctt catcggcgcg cgtgcggtgc 10980 tcggtctggg cgccgcgctg atcatgccga cgacgctgtc gctgctgccg gtcatgttct 11040 ccgacgagga gcggccgaag gccatcggag cggtggccgg tgcggcgatg ctcgcctatc 11100 cgctcggccc gatcctcggc ggctacctgc tcaaccactt ctggtggggc tccgtcttcc 11160 tgatcaacgt gccggtggtg atcctcgcct tcctcgcggt ctccgcctgg ctgcccgagt 11220 ccaaggccaa ggaggccaag ccgttcgaca tcggcggcct ggtgttctcc agcgtcggtc 11280 tcgccgcgct gacctacggc gtgatccagg gcggcgagaa gggctggacg gacgtcacca 11340 cgctggtgcc gtgcatcggc ggtctgctcg ccctcgtgct gttcgtgatg tgggagaagc 11400 gggtggcgga cccgctggtc gacctctcgc tgttccgctc ggcccggttc acctccggca 11460 ccatgctcgg caccgtcatc aacttcacga tgttcggcgt gctcttcacg atgccgcagt 11520 actaccaggc ggtcctcggc accgacgcga tgggcagcgg cttccggctg ctcccgatgg 11580 tcggcggtct gctcgtgggt gtgacggtcg ccaacaaggt cgccaaggcc ctcggcccga 11640 agaccgcggt cggcatcggc ttcgccctcc tcgccgccgc cctgttctac ggcgccacca 11700 cggacgtcag cagcggcacc ggcctggcgg ccgcctggac cgcggcctac ggactcggcc 11760 tcggcatcgc cctgccgacc gccatggacg ccgccctcgg cgcgctctcc gaggactccg 11820 ccggcgtcgg atccggcgtc aaccagtcca tccgtaccct cggcggcagc ttcggcgcgg 11880 ccatcctcgg ttccatcctc aactccggct accgcggcaa gctcgacctc gacggcgtgc 11940 ccgagcaggc acacggcgcg gtcaaggact ccgtcttcgg cggcctcgcg gtggcccggg 12000 cgatcaagtc caacggactg gccgactcgg tgcgttccgc gtacgtccac gccctggacg 12060 tggtgctcgt ggtctccggc ggcctcggac tgctgggtgt ggtgctggcg gtggtgtggc 12120 tgccccgcca tgttggtcag agcaccgcca agacagcaga atctgagcat gaagccgcag 12180 acgcagtctg accagggcaa aacagtgcct ggtctgagag aacgcaagaa ggcccggacg 12240 aaggccgcga ttcagcggga ggcggtgcgc ttgttcaggg aacagggcta caccgccacg 12300 accatcgagc agatcgccga agccgccgag gtcgctccca gcaccgtctt ccgctacttc 12360 gcgaccaagc aggacctggt cttctcgcac gactacgatc tgcccttcgc gatgatggtc 12420 caggcccagt cacccgacct gacgccgatc caggccgagc ggcaggccat ccgctcgatg 12480 ttgcaggaca tcagcgagca ggaactggcc ctgcagcgcg agcggttcgt cctgattctc 12540 tccgagccgg agctctgggg cgccagcctc ggcaacatcg gccagaccat gcagatcatg 12600 agtgagcagg tggccaaacg ggccgggcgc gacccgcggg accccgcggt ccgcgcctac 12660 accggagccg tgttcggagt gatgctccag gtctcgatgg actgggccaa cgatccggac 12720 atggacttcg cgaccacgct ggacgaggca ctccactacc tggaagacct gcggccctga 12780 ccgaaggggc gggcgcacac cacagagccc gccccggcca gacgtcgtac gaggcgccat 12840 cggccgtcgc gtacgacccc cgcgccccgg attcccccgc ggggcgcggg gtcaagggaa 12900 aagagacgac cgcacgcggc cactgttccc ccggctgccg cgtccggtcc aacctggcgt 12960 gctccggctt ccctcgacgg agcacgccag gggtctgtcc ggccctctcc cggcggctcc 13020 cgtcagacgc ccggccccgc cgtcagcgcc tcggtcacga cggccgccac ctgctcctga 13080 cagccgtcga ggtagaagtg cccgccgggc agcacccgca gatcgaacgc cgcgccggtc 13140 cgctcccgcc acgtggcggc ctgctccggc gacgtccgct cgtcggcgtc cccgatcagc 13200 gccgtgatcg ggcagtcgag ccggccgggt cccggcgcct cgtaggtggc cacggcccgg 13260 tagtcggccc gcagcgcggg caggacgagc tcctgcagct cgggactgcg gaagaaccgc 13320 tcgtcggtgc cgcccatcgc ccgcagatgg gccaggatgt ccgcgtcccc gaacgccccc 13380 gaacgccccg cgggacggta gggccgcgcg agccccccgg aaacgaacag gtgcacggga 13440 aggccgggcc cggccggtcc ccgcagccgc cgcgccacct cgaacgccac gatggcgccc 13500 aggctgtgcc cgaacagcgc gaatggcttc ccgtcgcacg gcaggtgggg cacgacgccg 13560 tcggcgagct cggccaccga cgccaggcac ggctccgcat gacggtcctg ccgccccgga 13620 tactgcacgg cgagcacctc gacgccgggc gcgagcagcc cggagagccc gaagtagtaa 13680 ctcgccgaac cgcccgcgaa cggaaagcag accagccgca ccggcgcctc tgccgcagcg 13740 tggtaccgcc gcaaccacac cccgtttccg gtggctgcac cgaactcgtc accgatctgt 13800 ggtgcccgcg ccgccgtgcc cctgtccatc gttctccctc tcctcgcgtc gctccgcggg 13860 cgctgtcctg ccccgccccg aaagcccgat gccggccaag ccccgatgct ggccaaaccc 13920 cgatgccggc caagccccga tgctggccgc ggcccatagc gcccggctaa agccgcaggc 13980 ggctagccgg ggtttggttc gcctttagac agcccaccca cgatgagccc ggtactcgaa 14040 gcgatctccg atttcggacc gggagcgccg ttgatgtttt gtggcagcca gttgttcagc 14100 gcccgaccgc agctgacgtg atggccgcat ccgcgtcagc gtccccctcg ggaccgagcg 14160 caggacccga cccgatcgcc gtcgtcggga tggcctgccg cctgcccgga gcacctgacc 14220 ccgacgcgtt ctggcggctg ctcagcgagg ggcgcagcgc ggtgagcacc gcaccgcccg 14280 agcggcggcg agccgactcc ggcctccacg ggccgggcgg ctacctggac cggatcgacg 14340 gcttcgacgc ggacttcttc cacatcagcc cgcgcgaggc cgtggcgatg gacccccagc 14400 agcggctgct cctcgaactg agctgggagg ccctcgaaga cgcgggcatc cggccgccca 14460 ccctggcgcg cagccgcacc ggcgtcttcg tcggcgcgtt ctgggacgac tacaccgacg 14520 tcctgaacct gcgggcgccg ggcgccgtca cccgccacac catgaccggc gtgcaccgca 14580 gcattctggc caaccgcatc tcgtacgcgt accacctggc cggtccgagc ctcaccgtcg 14640 acaccgcaca gtcctcctcg ctcgtcgccg tccacctggc ctgcgagagc atccgcagcg 14700 gcgactccga catcgccttc gcgggcggcg tcaacctcat ctgctcgccg cgcaccaccg 14760 agctggccgc ggcccgcttc ggcggtctct cggccgcagg ccgctgccac accttcgacg 14820 cccgcgccga cggtttcgta cgcggcgagg gcggcggcct cgtggtgctc aagcccctcg 14880 cggcggcacg gcgcgacggc gacacggtgt actgcgtgat ccgggggagc gccgtcaaca 14940 gcgacggtac gaccgacgga atcaccctgc ccagcgggca ggcgcagcag gacgtggtgc 15000 gcctcgcctg ccgacgggcg cggatcacgc cggaccaggt gcagtacgtc gaactgcacg 15060 gcaccggcac gcccgtcggg gacccgatcg aggccgccgc gctcggcgcc gccctcgggc 15120 aggacgccgc ccgcgccgtg ccgctggccg tcggctccgc caagacgaac gtcggccacc 15180 tcgaagccgc cgccggaatc gtcggactgc tcaagaccgc cctgagcatc caccaccggc 15240 ggctggcgcc gagcctgaac ttcaccaccc ccaatccggc catcccgctc gccgacctcg 15300 gcctgaccgt ccagcaggac ctggccgact ggccgcgccc cgaacagccc ctgatcgccg 15360 gggtgtcgtc cttcggcatg ggcggcacga acggtcacgt tgtcgtggcg gcggcgcccg 15420 attcggtggc ggtacctgag ccggtggggg tgcctgagcg ggtggaagtg cctgagccgg 15480 tggtggtttc tgagccggtg gtggtgccga cgccatggcc cgtgagcgct cacagcgctt 15540 ccgcgctgcg cgcgcaggcc ggtcgcctgc ggacgcacct cgccgcccac cgccccaccc 15600 ccgacgccgc gcgggtcggc cacgcgctcg ccaccacccg tgcgcccctc gcccaccgcg 15660 cggtcctgct cggcggcgac accgccgaac tgctgggctc cctggacgcg ctggccgagg 15720 gcgcggagac cgcgtccatc gtgcgcggcg aggcgtacac cgagggcagg acggccttcc 15780 tcttcagtgg gcagggagcg caacgcctcg gcatggggcg ggagttgtat gccgtgttcc 15840 ccgtcttcgc cgacgctctc gacgaggcgt tcgccgccct ggacgtacat ctggaccgcc 15900 cactgcgcga gatcgtcttg ggcgagaccg actcgggtgg gaacgtctcg ggtgagaatg 15960 tcatcggcga gggtgccgac catcaggcac tcctcgacca gaccgcctac acccagcccg 16020 cgctcttcgc gatcgagacg agcctgtacc ggctggcagc ctccttcggc ctgaagccgg 16080 actacgtcct cggccactcg gtcggcgaga tcgccgccgc gcacgtcgcc ggtgtcctct 16140 cgttgccgga cgcgagcgct ctggtggcca cgcggggacg gctcatgcag gcggttcgcg 16200 cgcccggcgc gatggccgcg tggcaggcca cggcggacga ggcggccgaa cagctcgccg 16260 ggcacgagcg gcacgtcacc gtggccgccg tcaacggccc cgactccgtg gtcgtctccg 16320 gcgaccgcgc caccgtcgac gaactgaccg ccgcctggcg gggacgcggc cgcaaggccc 16380 accacctgaa ggtcagccac gccttccact ccccgcacat ggaccccatc ctcgacgagc 16440 tgcgcgcggt cgccgccggc ctgaccttcc acgagccggt cattcccgtc gtctccaacg 16500 tcaccggtga actggtgacc gcgaccgcga ccgggagcgg cgccgggcag gccgaccccg 16560 agtactgggc gcggcatgcg cgcgagcccg tgcggttcct gtccggggtg cgggggctgt 16620 gcgagcgcgg ggtgaccacg ttcgtcgagc tcggcccgga cgcaccgctg tccgcgatgg 16680 cccgcgactg cttccccgcc cccgcggacc ggagccgtcc gcgccccgcc gccatcgcca 16740 catgccgccg cgggcgcgac gaggtggcca cgttcctgag gtcgctggcc caggcgtacg 16800 tccgcggcgc cgatgtcgac ttcacccggg cctacggcgc caccgccacg cgccgcttcc 16860 ccctccccac gtatcccttc cagcgcgagc gccattggcc tgccgctgcc ggggtggggc 16920 agcagccgga gaccccggaa cttccggaat cctcggagtc ctcggagcag gcagggcatg 16980 agcgggagga gggggcgcgc gcgtggggcg ggcctgaagg gcggcttgcc gggctctccg 17040 tgaacgacca ggagcgggtc ctcctcggcc tggtcaccaa gcacgtggcc gtcgtgctcg 17100 gggacgcctc gggcacggta caagccgccc gcaccttcaa gcagttgggc ttcgactcga 17160 tggccgccgc cgagctgagc gaacggctcg gcacggagac gggcctgccg ttgcccgcca 17220 ccctcacctt cgactacccg acccctctgg ccgtcgccgc gcacctgcgc gcggagctca 17280 ccggtacgcc cgccccggcc ggctccgcgc ccgccacggg cgccctcggc gcgggtgacc 17340 tcggcacgga cgaggacccg gtcgccatcg tggccatgag ctgccgctat cccggcggcg 17400 caggcacgcc cgaggacctg tggcggctgg tcgcggacgg cgccgacgcg atcggagact 17460 tccccaccga ccgcggctgg gacctggcgc ggctgttcca ccccgacccc gaccggtcgg 17520 gcaccagctg cacgcggcag ggcggattcc tgtacgacgc cgccgacttc gacgccgagt 17580 tcttcgacat cagcccgcgc gaggccctgg ccgtcgaccc gcagcagcgg ctgctcctcg 17640 agtgcgcctg ggaggccttc gaacgggcgg gcctggaccc gcgggcgctc aagggcagcc 17700 ccaccggcgt gttcgtcggc atgacggggc aggactacgg cccccgtctg cacgagccgt 17760 cccaggccac cgacggctat ctgctgaccg gcagcacgcc gagcgtggcc tcgggccgcc 17820 tgtcgttcag cttcggcctt gaggggcccg ccctgacggt ggacacggcc tgctcgtcgt 17880 cgctggtcac gctccatctc gcggcgcagg cgctgcggcg cggcgagtgc gacctggccc 17940 tcgccggcgg cgccaccgtc ctggccacgc cgggcatgtt caccgagttc tcgcggcagc 18000 ggggcctggc ccccgacggc cgctgcaagc cgttcgcggc gggcgccgac ggcacgggct 18060 gggccgaggg cgtgggcctg gtcctcctcg aaaggctctc cgaggcccgg cgcaaggggc 18120 acgccgtcct cgcggtgatc cggggttcgg cgatcaacca ggacggcgcg agcaacggcc 18180 tgaccgcgcc caacggcccc tcgcagcaac gcgtcatccg tgccgcgctc gcggccgccc 18240 ggctcaccgc ggacgaggtc gacgtagtgg aggcgcacgg caccggcacc acgctcggcg 18300 acccgatcga ggcgcaggcc ctgctcgcca cgtacggcca agggcgttcg gcggagcggc 18360 cgttgtggct cgggtcggtg aagtcgaaca tcggtcacac gcaggccgcc gcgggtgtcg 18420 cgggcgtcat caagatggtg atggcgatgc gccacgacct gctccccgcc accctgcacg 18480 tcgacgagcc gagtggccac gtggactggt ccaccggcgc ggtgcgactg ctcaccgagc 18540 cggtcgtctg gccgcgcggc gaacgtccgc gccgcgccgc ggtgtcgtcc ttcggcatct 18600 ccggcacgaa cgcgcacctg gtgctcgaag aggcggggca ggacgagtac gttgcgggag 18660 ccgccgacga cgccgggccg gtggacggtg ctgtgctgcc gtgggtggtt tccggacgga 18720 ccggagcggc gctgcgcgaa caggcccgcc gtttgcgtga gttggtgacc ggcggctcgg 18780 ccgatgtctc tgtgtccggg gtgggccggt cgctggtcac cacgcgggcg gtgttcgagc 18840 accgggccgt ggtcgtgggc cgcgaccggg acacgctgat cggcggcctc gaggcccttg 18900 cggcgggtga cgcgtcgccg gacgtcgtgt gcggggtcgc gggcgatgtc ggccccggcc 18960 cggtgctggt gttccccggg cagggctcgc agtgggtggg catgggagcc caactccttg 19020 gcgagtccgc ggtgttcgcg gcgcggatcg acgcgtgcga gcaggcgctg tccccgtacg 19080 tcgactggtc actgacagag gtcctgcgcg gggacgggcg cgaactgtcg cgcgtcgacg 19140 tcgtccagcc cgtgctgtgg gcggtgatgg tctcgctcgc cgccgtctgg gcggaccacg 19200 gcgtcacccc ggccgccgtc gtcgggcact cccagggaga gatcgccgct gtggtcgtcg 19260 ccggcgcgct caccctggag gacggcgcca agatcgtggc cctgcgcagc cgggcgctgc 19320 gtcagctctc gggcgggggc gccatggcct ccctcggggt gggccaggaa caggcagccg 19380 aactcgtcga gggccacccc ggagtgggca tcgccgccgt caacggcccg tcatcgaccg 19440 tcatttcagg cccgcccgag caagtcgccg ccgtcgtcgc cgacgccgag gcgcgcgagc 19500 tgagaggccg cgtcattgac gtggactacg cctcgcacag cccccaggtc gacgccatca 19560 ccgacgaact cacccacacc ctgtccggcg tccgccccac cacggccccg gtggcgttct 19620 actcggccgt gaccggaacc cgcatcgaca cggcgggcct cgacaccgac tactgggtca 19680 ccaacctgcg ccgcccggtc cggttcgccg acgccgtcac cgcgctcctc gccgacggcc 19740 accgggtctt catcgaggcc agcagccacc ccgtcctcac cctcggcctc caggagacct 19800 tcgaggaggc cggggtcgac gccgtcaccg tccccaccct gcggcgcgag gacggcggcc 19860 gggcacgcct ggcccgctcg ctggcacagg ccttcggcgc cgggtgcgcg gtgaggtggg 19920 agaactggtt tccggccacc ggtacgtcca ccgtggagct gccgacgtac gccttccagc 19980 gtcgccgtta ctggctggag gcccccacgg gcacccagga cgcggcgggc ctgggcctcg 20040 ccgctgcggg gcacccgctc ctcggggcgg ccaccgagat cgcggacggc gacatccgcc 20100 tgctcaccgg ccgtatcagc aggcacagcc acccctggct cgctcagcac accctcttcg 20160 gtgccgcggt cgtgcccgcc tccgtcctcg cggaatgggc gctgcgcgcc gccgacgagg 20220 ccggctgccc gcgtgtcgac gacctcacgc tgcgcacccc gctggtgctg cccgagaccg 20280 cgggcgtgca ggtgcagatc gtggtcggcc cggccgacgc gcgggacggg caccgcgact 20340 tccacgtcta cgcccgcccc gacggcaagg acgcctctga gggcgagggc atcgccgagg 20400 gcgagggtgc ctctgagggc gagggtgcct ccggcggcac cgatgcgccg tggacctgcc 20460 atgccgacgg ccgactggtc gccgagccca ccggcacggc ctcggaggac tccccggaca 20520 cggtgtggcc gccgcccggc gccgaacccg tcgacctggg cgacttctac gagcgggccg 20580 ccgccaccgg agtcggctat ggaccggtct tcacggggct gcgcgccctg tggcggcggg 20640 acggcgagct gttcgccgag gcggtgctgc cgcaagaagc cccggaaacc gccgggttcg 20700 gcatgcaccc ggcgctcctc gacgccgcac tgcaccccgc actcctcggc gagcggccgg 20760 ccgaggagga caaggtgtgg ctgccgttca cgctgaccgg agtgaccctg tgggccaccg 20820 gtgccacctc tgtacgcgtc cgtctcaccc cgctggacga cgaccccgac gcgtcggcgg 20880 acgggcgggc ctggcgggtc ggcgtgagcg acccgaccgg cgcggaggtg ctgacctgcg 20940 aggccctggt cgcggtggcg gcgggccgcc gcgagctgcg ggccgcgggg gagcgggtgt 21000 ccgatctgta cgcggtggag tgggtgccgg tgccgggccc ggggccggtg ggtgagggtg 21060 ctgacttctc gggctgggcc ggtctggggg agtgcgggga gcgttgggag tgcgtggggc 21120 gcgtggagcg ctggtacgag gacctggacg ctctcggcgc ggctgtcgag ggtggggctt 21180 cggtgccctc tgtcgttctc gccaccgcgg ctgccgcccc tggtggagcg ggcgacggag 21240 ccgccgatgc gctgagcgcg gtgcggtgga ccggcgcgct cctcgatcag tggctcgccg 21300 acgcgcggtt cgccgacgcc cggctggtgg tgatcacgtc cggcgcggtc gccacgggtg 21360 acgatttcct tcccgacccg gccgccgcgg cggtacgagg actggtcgag caggcgcagg 21420 tcaggcaccc cggccgcatc ctcctcgtcg acacggaagc cggggccggg ctcggggtcg 21480 gcgccggagt ggatgacgcg ctcctggaac aggccgtggc catggctctc ggcgccgacg 21540 aaccgcaact cgccctgcgc gcggggcggg tcctggcgcc ccgcctcacc gcaccccagg 21600 atgcggccgt caccgaagcg gcgcgaccgc tcgacccgga cggcaccgta ctcatcacag 21660 ggccggccgg tgctccggtg gccgacctcg ccgaacacct cgtacgcacc gggcagtgca 21720 ggcatctgct gctcctgcct ggagacggtg aactggagga aatggccgag gagttgcggg 21780 gcctcggcgc caccgtggac ctgagtaccg ccgacccggc ggacccgacc gccctcgccg 21840 aagtggtcgc cgccgtcgag ggggaccatc ctcttacggg ggtcatccac gccaccggag 21900 tcgtggacgc gttcgatccc ggcgactcgg cgagcgactt gatgatcgac tcggcgagcg 21960 attcgttcgc cgaggcatgg tcgtcgaggg cgggcgtcac cgccgcactg cacaccgcga 22020 ccgcccacct tcccctggac ctgttcgccg tcctgtcccc ggcgggcgcg gacctgggca 22080 ttgcccggtc ggcggccgcc gcgggcgccg acgccttcag cgcggcactc gccctgcgcc 22140 ggcacacgac cgtcacgacg gacacgacag ccccgccgcg cacgacagcc ccgccgcgaa 22200 cgacagcctc gccgcgcacg acagccctgt cgtcgtcgcg cacgacgggc gtggccctcg 22260 cctacgggcc gcccaccgcg ccgaggcccg gcatcaaggg gacggcgccc ggtcggatcc 22320 ccgtgctgct cgacgccgct cgcgctcacg ggggcggttc gcccctgctc ggggcccgct 22380 tggccgcgcg tgccctggcc gccgagtccg ccgccgaggg cgtcgccggc ctgcccgcgc 22440 cgctgcgcgc gctggcagtg gccgcagccg cggccggagc accgacccgg cgcaccgccg 22500 ccgaccgcaa gccccccgcg gactggccgg cccgactggc ccccctgtcc gcccccgaac 22560 aactccgtct gctcatcgac gccgtacgca cccacgccgc cgcggtcctc ggccgcaccg 22620 acccggaagc gctgcgcggg gacgccacct tcaagcagct cggccttgac tcgctgaccg 22680 ccgtggagct gcgcaaccgg ctcgtggagg acaccggtct gcgcctgccc accgccctcg 22740 tctttcgcta cccgaccccc gcggcgatcg ccgcgcacct ccgcgagcgg ctgaccagcc 22800 cgagcgagac gaccgccaca cagaggtccg gagggcagac gcccgcagcg gggcaggcgt 22860 cgtccgcgct cgcccccggc ggatcggccg ccggaccgcc cgccgcagac accgtgctga 22920 gcgacctgac ccgcatggag aacaccctct ccgtgctcgc cgcccagctg ccccacaccg 22980 agacgggtga gatcaccacc cggctcgaag cgctcctcac gcgctggaag accacgaacg 23040 ccacggcgaa cgacagcggc gacggcaacg gcggcgatga cgacgccgcc gaacgcctca 23100 aggccgcgtc cgccgaccag atcttcgact tcatcgacaa cgagcttggt gtcgggcacg 23160 gcacctcgcg cgtgaccccc actccgaagg ccgggtgacc gcacatggcg agtgaagagc 23220 aactggtcga atatctgcgc agggtgacca ccgagctcca tgacacgcgt cggcgcctgg 23280 tgcaggagga ggaccgcagg caggaaccgg tggccctggt cggcatggcc tgccgcttcc 23340 cgggcggcgt ggcctcaccg gaggacctct gggacctggt cgccgcgggc aaggacgcca 23400 tcgaggactt tcccaccgac cggggctggg acctggaggc gctctacgac ccggacccgg 23460 ccgcgtacgg gaccagctat gtccgccacg gcgggttcgt ggacgacgcg ggctccttcg 23520 acgccgactt cttcggcatc agcccgcgag aagccctggc gatggacccg cagcagcggc 23580 tgatgctgga gacgtcctgg gagctgttcg agcgcgccgg catcgaaccc gtctccctca 23640 agggcagccg tacgggcgtc tacgccgggg tgtccagcga ggactacatg tcccaactgc 23700 cccgcatccc cgaggggttc gaggggcacg ccaccaccgg cagcctcacc agcgtcatct 23760 cgggccgggt cgcgtacaac tacggcctcg aaggcccggc cgtcaccgtc gacacagcct 23820 gttccgcctc gctcgtcgcc atccacctgg cgagccaggc gctgcgccag cgtgagtgcg 23880 acctcgccct cgcgggcggt gtgctcgtac tgtccagccc gctcatgttc accgagttct 23940 gccgccagcg gggccttgct cccgacggcc gctgcaagcc gttcgccgcc gcggcggacg 24000 gcaccggctt ctcggagggc atcggtctgc tcctcctgga gcgcctgtcc gacgcgcgcc 24060 gcaacggcca caaggtgctc gcggtgatcc gcggctccgc cgtcaaccag gacggcgcga 24120 gcaacggcct gaccgccccc aacgacgccg cgcaggaaca ggtcatccgc gccgccctcg 24180 acaacgcccg cctcaccccg tccgaggtgg acgccgtcga ggcgcacggc accggcacca 24240 aactgggcga ccccatcgag gccggagcgc tgctcgccac ctacgggcaa caccgcgccc 24300 ggcccctcct cctcggctcc ctcaagtcca acatcggcca cacccacgcc accgcgggcg 24360 tcgccggtgt catcaagacc gtcatggcga tccgcaacgg tctgctcccc gccaccctcc 24420 acgtcgagga actgagcccg cacgtcgact gggacgcggg cgcggtcgag gtcgtcacgg 24480 agcccacccc gtggcccgag accggccacc cccggcgcgc gggcgtctcc gcgttcggga 24540 tctccgggac gaatgcgcac ttgatcctgg aggaggcgcc gccggaggag gatgtgcccg 24600 cccccgtggt tgtggagtcg ggcggggtcg ttccgtgggt ggtgtccggg cggacgccgg 24660 aggcgctgcg tgaacaggcc cggcgactcg gcgagttcgt ggcaggcgac acggacgcac 24720 tgccgaacga ggtcggctgg tccttggcca cgacccggtc ggtgttcgag caccgggctg 24780 tggtcgtggg gcgtgaccgg gatgcgttga cggctggcct gggggcgttg gctgcgggtg 24840 aggcttcggc gggtgtggtg gccggggtgg ccggtgatgt gggtcctggg ccggtgttgg 24900 tgtttccggg gcagggggcg cagtgggtgg gcatgggtgc ccagctgttg gacgagtctg 24960 cggtgttcgc ggcgcggatc gcggagtgtg agcgggccct gtcggcgcat gtggactggt 25020 cgctgagtgc ggtgttgcgc ggggacggga gtgagctgtc ccgggtggaa gtggtgcagc 25080 cggtgctgtg ggcggtgatg gtctcgctgg ctgcggtgtg ggcggattac ggggtcactc 25140 cggctgccgt gatcgggcac tcgcagggtg agatggctgc cgcgtgtgtg gcgggggcgc 25200 tgtcgctgga ggatgcggcg cggatcgtag cggtacgcag tgacgcgctt cgtcagctgc 25260 aagggcacgg cgacatggcc tcgctcagca ccggtgccga gcaggccgct gagctgatcg 25320 gtgaccggcc gggcgtggtc gtcgcggcgg tcaatgggcc gtcgtctacg gtgatttcag 25380 ggccgccgga gcatgtggca gccgtggtcg cggatgcgga ggcacgtggt ctgcgcgccc 25440 gtgtcatcga cgtcggctat gcctcgcatg gcccccagat cgaccagctc cacgatctgc 25500 tgaccgaacg cctggccgac atccggccca cgaacacgga cgtggccttc tattcgacgg 25560 tcaccgccga gcgcctgacg gacaccacgg ccctggacac ggattactgg gtcaccaacc 25620 tccgtcagcc cgtccggttc gccgacacca tcgaagccct tctcgcggac ggctaccgcc 25680 tgttcatcga ggccagcgcc caccccgtgc tgggcctggg catggaggag accatcgagc 25740 aggcggacat gcccgccacc gtcgtcccca ccctccgccg cgaccacggc gacaccaccc 25800 agctcacccg cgccgccgcc cacgccttca ccgccggcgc cgatgtcgac tggcggcgct 25860 ggttcccggc cgaccccgcc ccccgcacga tcgatctccc cacctacgcc ttccagcgcc 25920 gccgctactg gctggccgac acagtgaagc gggacagcgg atgggacccg gccgggtcgg 25980 ggcatgccca gttgccgacc gcggtcgccc tcgccgacgg gggagtggtg ctgaacggcc 26040 gggtgtccgc cgagcgcggt ggctggctgg gcgggcatgt ggtggcgggg acggttctgg 26100 tgccgggtgc ggcgttggtg gagtgggtgt tgcgggccgg tgatgaggcg ggttgcccct 26160 cgcttgagga gttgacgctc caggcgccgt tggtgttgcc cgagtcgggt gggttgcagg 26220 ttcaggtggt cgtgggtgcg gctgatgagc agggcggccg tcgtgacgta catgtgtatt 26280 cgaggtctga gcaggacgcg tcggcggtgt ggcagtgcca tgccgtcggt gagctcgggc 26340 gcgcgtcggt ggcgcggccg gtgcggcagg ccgggcagtg gcctccggcg ggggccgagc 26400 cggtggaggt gggcggcttc tacgaggggg tcgcggccgc cggttacgag tacggtccgg 26460 cgttccgtgg gctgcgcgcg atgtggcggc acggtgatga cctccttgcg gaggtcgagc 26520 tgccggagga ggccggttcg ccggccggtt tcggcatcca cccggcgctg ctggacgccg 26580 ccctgcaccc gctgctcgca cagcggagcc gggacggggc cggggcgggg gcccacggcg 26640 ggcaggtgct gctgcctttc agctggagcg gtgtttccct gtgggccagc gaggccacca 26700 ctgtgcgggt gcggctcacc gggctgggag gaggggacga cgagacggtg tccctgacgg 26760 taaccgaccc cgccggtggc cccgtggtgg acgtggcaga gctgcggttg cggtcgacga 26820 gcgcccggca ggtgcggggt tcggcaggcc ccggcgcgga cgggctctac gagctgcggt 26880 ggacaccgtt gcccgagccg cttcccgtac cggcccccgc gaacggtcgc gatgtggccg 26940 ccgacctgtc cggatgcgcg gtgctcggcg aactggtcgc ggaaccgggc ccgggcatcg 27000 acctggaggg ctgcccctgc tacccgggcg tcggcgcgct cgccgacaac gcctccccgc 27060 cctccatgat cctcgccccc gtgcacagcg acaccacagg cggcgacgga ctcgccctga 27120 cggaacgggt gttgcgcgtc atccaggact tcctggctgc accgagtctg gaacagaaac 27180 agacgcgcct ggccttcgtg acccggggcg cggcggacac aggtagcacg acgggaggct 27240 cggctgcccc ggcagaggca gtcgacccgg cggtcgcggc cgtatggggc ctagtacgca 27300 gcgcgcagtc ggagaacccc ggccgcttcg tactgctgga caccgacgcg cccctcgacc 27360 aggcgtccgt tgcccctctc gtggacgcgg tgcggtctgc cgtggaggcg gacgagcccc 27420 aagtcgccct gcgcggggga cggttgctcg tgcccaggtg ggcgcgggcc ggcgagcccg 27480 tcgagctggc cgggccggcc ggagcgcggg cgtggcggct ggtgggcgga gactccggga 27540 cgctggaggc cgtcgtggcg gaggcttgcg acgacattgt gctgcgcccg ttggcgccgg 27600 gccaggtccg cgtcgccgtc catacggccg gggtcaattt ccgtgacgtc ctgatcgccc 27660 tgggcatgta cccggacccg gacgcgctgc ccggcaccga ggcggccggc gtggtgacgg 27720 aggtcgggcc gggcgtcacc cgtctgtcgg tgggcgaccg cgtgatgggc atgatggacg 27780 gcgccttcgg cccgtgggcc gtcgccgacg cgcgcatgct ggccccggtc ccgcccggct 27840 ggggcacccg gcaggcggcc gccgctcccg ccgcgttcct gacggcttgg tacgggctgg 27900 tggagctggc cggtctgaag gcgggcgagc gtgtgttgat ccatgccgcc acgggtggtg 27960 tggggatggc ggcggtgcag atcgcccggc atgtgggtgc cgaggtgttc gccaccgcga 28020 gtccgggcaa gcacgccgtg ctggaggaga tgggcatcga cgccgcccac cgcgcctcgt 28080 cgcgcgacct cgccttcgag gacgccttcc ggcaggccac cgacggccgt ggcgtggacg 28140 tcgtcctcaa cagcctcacc ggtgaactgc tcgacgcgtc cctgcgattg ctcggcgacg 28200 gcgggcgctt cgtggagatg ggcaagagcg atccgcgcga ccccgagctg gtcgcgctgg 28260 agcaccccgg ggtgtcgtac gaggccttcg acctcgtcgc cgacgccggg cccgagcggc 28320 tcgggctgat gctcgacagg ctcggcgagc tcttcgccgg cggatcactg gtaccgctgc 28380 cggtcaccgc atggccgctg gggcgggcgc gagaggcgct ccgccacatg agtcaggcga 28440 ggcacaccgg caagctggtg ctcgacgtgc ccgcgccgct cgaccccgac ggcaccgtcc 28500 tcgtcaccgg gggtaccggc accatcggcg ccgccgtggc cgaacacctg gcgcgtaccg 28560 gggagagcaa gcacctgctc atcgtcagcc gcagcgggcc ggccgcccac ggcgccgagg 28620 aacttgtctc tcgtatagcc gagttcgggg ccgaagccac cttcgtcgct gccgacgtga 28680 gtgagcccga cgcggtcgcc gccctgatcg aagggatcga tccggcccat ccgctgaccg 28740 gtgtcgtgca tgccgccgga gtactcgaca acgctctgat cggctcccag accaccgaaa 28800 gcctcacccg cgtatgggcg gcgaaggccg ccgccgcgca gcaactccac gaggccacga 28860 gggagtcgag gctgggactg ttcgtgatgt tctcctcctt cgcctccacc atgggcaccc 28920 cagggcaggc caactactcc gccgccaacg cctattgcga cgcgctggcc gctctccgac 28980 gcgcggaggg gctcgccggc ctgtccgtgg cgtgggggtt gtgggaggcc accagcggcc 29040 tgaccgggac gttgtcggcg gccgaccggg cccgcatcga ccggtacggc atcaggccga 29100 ccagcgcggc acgcggctgc gccctgctgg cagcggcacg cgcccacggg cgccccgacc 29160 tgctcgccat ggacctggac gcccgcgtac ccgccgcgtc cgacgctccg gtccccgccg 29220 tgctgcgcac tctggcggcc gccggagcgc ccgccaccgc ccgtcccacc gcggcggcgg 29280 ccgctgacgg ggcgacggac tggtccggca ggctcgccgg cctcaccgag gaggcacggc 29340 tcgaactcct caccgagttg gtgtgcaccc acgcggcagg ggtgctcggg cacgccgacg 29400 cgggcgcggt ccaggtggac gcgccgttca aggaactcgg cttcgactcg ctgaccgccg 29460 tcgaactgcg caaccggatc gccgccgcga ccggcctgaa actgcccgcc gccctcgtct 29520 tcgactaccc gcaggctcgc gttctcgccg cccacctggc cgaacggctc gtcccggagg 29580 gcgcgggggc catgggcggt gtgagcggtg cggagggcgt gagggacgcg tacggggcag 29640 gcggtccggg cggcgacatg accgcccagg tcttgctgga ggtggcccgc gtcgagcaca 29700 ccctgtccgc cgccgtcccg cacggcctgg accgggcggc cgtcgcggcc cgcctggagg 29760 cgctgctcgc ccgctgcacg gcgacgacgg cggccacggg ggccgcggga gccgcggtgg 29820 agggtgacgg cgacagcgac ggcgacggcg ccgtggatca gctggagacg gccaccgccg 29880 agcaagtact ggacttcatc gacaacgaac tcggggtgtg agccgcgtgc cggccgcaca 29940 ccaggcgatc acgggcgggg agctgcagcg cacatggtga gcgaagagaa actggtcgac 30000 2 30000 DNA Streptomyces cinnamonensis Nucleotides 30001 - 60000 of the monensin biosynthetic gene cluster 2 tacctcaagc gtgtctccgc ggacctgcac gccacccggc agcggctgcg cgaggcggag 60 gagcgcggcc aggaacccgt ggccgtggtg gaggccgcct gccgctaccc cggcggcatc 120 cgcacccccg aagacctgtg ggacctggtc gccgcgggcg gcaacgccct gggcgccttc 180 cccgacaacc gcggctggga cctgcgacgc ctcttccacc ccgaccccga ccaccccggg 240 acgacctacg cccgcgaggg cggcttcctc cacgacgccg acctgttcga cccggagttc 300 ttcggcatca gcccccgcga ggccgcggtc ctcgacccgc agcagcgact gctcctggag 360 tgcgcctggg aggcactgga gcgcgcgggc atcgacccgc ggtccctcca gggcagccgt 420 accggcgtgt acgcgggtgc cgccctgccc ggcttcggca ccccgcacat cgaccccgcc 480 gccgagggcc acctggtcac cggcagcgcc ccgagcgtcc tctcgggccg gctcgcctac 540 accttcggcc tcgaagggcc cgcggtgacg atcgacaccg cctgctcgtc gtcgctcgtc 600 gccgtgcacc tggcggccca cgcgctgcgg cagcgcgagt gcgatctggc gctcgcgggc 660 ggtgtcaccg tcatgaccac cccgtacgtg ttcaccgagt tctcgcgcca gcgcggcctg 720 gccgccgacg gccggtgcaa gcccttcgcg gccgccgcgg acggcacggc cttctccgag 780 ggcgccggac tcctcgtact ggaacgcctc tccgacgccc gccgggccgg ccaccgggtg 840 ctcgccgtca tccgcggctc ggccgtcaac caggatggcg cgagcaacgg cctcaccgcc 900 cccaacggcc ccgcccagca gcgcgtgatc cgcgccgccc tcgccggggc gcggctctcg 960 cccgcggagg tggacgcggt cgaggcgcac ggcaccggca cccggctggg cgaccccatc 1020 gaggccgacg cgctcctcgc cacctacggt caggagcgcc acgggggccg gccgctgtgg 1080 ctcggctcgg tgaaatccaa catcggccac acgcagggcg cggccggtgc cgcgggcctg 1140 atcaagatgg tccaggcact gcggcacgag acgctgcccg ccacgttgta cgccgacgag 1200 cccaccccgc acgccgactg ggagtcgggc gcggtgcgcc tgctcagcgc gccggtcgcc 1260 tggccgcgcg gggagcacgg ggagcacacc cgcagggccg gcatctcctc cttcggcatc 1320 tccggcacga acgcccacct catcctggag gaggcgcccg cggccgacgc cgaaggagcg 1380 ggtggcgacg gcgatggcga cgggggaggg gtgcggccgg tggtgcgggt cggcgccacg 1440 ggcccccgcg aagagcaggg ccaaggacag ggccaagagc agcaccaaca gcaacgtcag 1500 cagcggcagc ggtcgtcgat gatgccgacg ccgcacctcc cgtggctgct gtccgcccgc 1560 agccccgccg cgctccgcgc ccaggccgac gcgctggcga accatgtcgc ccacgcggac 1620 cactccatcg ccgacatcgg cggcacactg ctgcgccgca ccctgttcga gcaccgggcg 1680 gtcgtcctcg gaaccgaccg tgatgagcgt gccgcagcgc ttgccgccct cgcggcagga 1740 cgcgcacacc ccgcgctgac ccgggccgca gggccggcga ggaacggcgg caccgccttc 1800 ctgttcaccg gccagggaag ccaacgccca ggcatgggca ggcagttgta cgacaccttc 1860 gacgtcttcg ccgagtcgct cgacgagacc tgcgcccggc tcgaccccct gctcgaacag 1920 ccgctgaagc ccgtcctgtt cgcccccgcc gacaccgcgc aggccgccgt gctgcacggg 1980 accggcatga cgcaggccgc gctgttcgcc ctcgaagtcg ccctgtaccg ccaggtcacc 2040 tccttcggga tcgcccccag ccacctgacc gggcactccg tcggcgagat cgccgccgcc 2100 cacgtcgccg gggtgttctc cctggcggac gcctgcacgc tggtcgcggc ccggggccgc 2160 ctcatgcagg ccctgcccgc aggtggcgcc atgctcgccg tccaggcggc cgaggacgac 2220 gtactgccgc tgctcgccgg gcaggaggaa cgtctctccc tcgccgccgt caacggcccc 2280 accgccgtcg tcgtgtccgg tgaggccgct gccgtcgggg aggtggagaa ggcgctgcgc 2340 gggcgcggac tgaagaccaa gcggctcaac gtcagtcacg ccttccactc gccgctcatc 2400 gagccgatgc tcgacgactt ccgcgaagtg gcccgcgggc tgaccttcca cgcgccgacg 2460 ctgcccgtcg tctccaacct caccggccgc ctcgccgacg cggagctgat ggccgacgcc 2520 gagtactggg tgcggcacgt acgccggccg gtgcggttcc acgacgggct gcgcgctctc 2580 agcgagcaag gcgtcgtgcg ctacctggag ttggggcccg acccggtcct cgccaccatg 2640 gtccaggacg gtctcccggc cccggcggag ggagaggagc ccgagccggt cgtcgccgcg 2700 gcgctgcgct ccaagcacga cgagggacgc accctgctgg gtgccgtcgc cgcgctccac 2760 accgacggac agccggccga cctcaccgcc ctcttccccg ccgacgccgg gcaagtgccg 2820 ctccccacct accggttcca gcggcgacgg tactggcgcg tcgcgcccga cgccgccgcg 2880 ccggcccgcg ccgccggcct ccaggagacc ggccacccgc tgctgcccgc cgtcatccgg 2940 caggccgacg gcggcatcct gctcgcggga cgcctgtccc tgcgtacgca tccatggctc 3000 gccgaccaca ccatcgcggg cggcgtcccg ctgcccgcca ccgccttcgt cgaactcgcc 3060 ctgctcgcag ggcggcacgc cgcctgcgac acgatcgacg atctgacgct ggagacgccg 3120 ctgctgctcg acgacaccgg taccggtgtc ggggcggctg tgggcgcggg cgccgatgcc 3180 ctcgtcgatg ccatagaagt gcagcttgcc ctcggcgctc ccgacggttc cggccgccgt 3240 gctctcaccg tccactcccg tcctgccgac gatgcggctg acgacggcga cgcggccgac 3300 gcggccgatg cggcaggccg gggaggcccg ggcggctcgg gtgacctggg cgatcctggc 3360 gatccgggcg atctgggcga cggcgggggc tcccgcggct ggcgccgtca cgccaccggc 3420 atcctcagcg ccggcccggc cgccgaaccg gccgcccccg acgccgctcc ctggccgccc 3480 gccgacgcca ccgccctcga cgtcgacgcg ctgtacgccc ggctcgacgc gcagggctac 3540 agctacgggc ccgccttccg ggccgtccac gccgcctggc ggcacggcga cgacctctac 3600 gccgatgtcc gcctcgccga cgaacagcgc gctgaagccg acgcgttcgc cctccacccg 3660 gccctgctcg acgccgccct gcatgccgtc gacgagctgt accgcggcag tgaggggcgg 3720 gggcaggagc aggggcaggg tggtcaggag ccggagcagg gccgtggcga cgcggacgcc 3780 ccggtacggc tgccgttctc cttcagcgac atacgccacc acgccaccgg ggccacacgg 3840 ctgtgggtcc gcctcagccc ccagggcgac gatcggctgc ggctgtccct gaccgacggc 3900 gagggcgggc aggtcgcgac agtcgacgcc ctccaactgc ggttgatccc cgccgaccgg 3960 tggcgcgcgg cccgccccac cacagccgcc cccctgtacc acctggactg gcacgagctg 4020 ccgttgcccg agccggccga gacggacccg gccgcccact cctgggctgt gctcggagcg 4080 cacgacgcgg gcctcgctcc cgccgcgcac tacccggacc tggcggccct gaaagccgcc 4140 gtcgaggccg gcgagcccgt gccggacatc gtcttcgcac cgttccccgc gcaggggacg 4200 gagaccgatg tcccggctca ggtacgagcc cacgcccggc acgccctgga gctgctgcgc 4260 gactggctca ccacggaagc tttcgccgcc gcccgcctcg tcgtcctcac gaccggtgcg 4320 gtcaccgccc gcccagagga cgggcccgcc gacctggcca ccgcacctgt atggggcctg 4380 gtccgagccg cccaggccga acaacccgac catgtcgtcc tggtggacat cgacaaggac 4440 atcgataagg acaccgacga ggagaccgac caggccaccg acgcgggcac cgcatcgcgc 4500 cacgctctgc ccgccgcctt ggccgcggcg gccgcccaag ccgagacaca gctcgccctg 4560 cgcgcgggca ccgtgctcgt gccgcgcctc gccgtcgtcc cgccccggac cgacacccca 4620 gcgctgcacg ccaccgcccc ggagagcacc acggacactg tggactccac gggcatcgcg 4680 ggcgctgcgg aatccggcgg caccgtcctg atcaccggcg gaaccggcgg cctcgggcag 4740 gccgtcgccc gtcacctcgc cgccgcgcat ggcgcccgcc acctgctcct cgtcagccgc 4800 aggggcgacg ccgccgaggg cgtcgccgag ttgcgcgccg acctcgcgga cgacggcgtc 4860 gacgtacgcg tcgccgcctg cgacatcacc gaccgcgacg cgctggccgg gctcctcgcg 4920 gacatccccg ccgcgcaccc gctcaccgcg gtcgtgcaca ccgcgggcgt catcgacgac 4980 agcctcatca cggcgatgac ccccgagcgg ctcgacgccg tcctcgcacc caaggccgac 5040 gcggcctggc acctgcacga actcacccgc gacaaggacc tgtcggcctt cgtcctcttc 5100 tcctcgggcg cctccgtcct cggcaacggc ggccaggcca actacgcggc cgccaacacc 5160 ttcctcaaca ccctcgccga acaccgccgc gcggccggcc tcgccgccac ctccgtggcc 5220 tggggcctgt gggagtccgc gtccggcggc atggccgccc ggctcggcga cgccgaccgc 5280 gcccgcatcc accgcaccgg cgtgacgggc ctgaccgacg agcaggccct ggccctcttc 5340 gacgcggccc tgaccgccga gcaccccacg gtcctcgcca cccgcttcga ccgcgccgtg 5400 ctgcgcggcc aggccgccgc ccgcaccctg cagcccgccc tgcgcggcct ggtacgcact 5460 ccgcgcccca ccgcgtccgc cggggccatc gggtccaccg cagccaccgg gtccgccacg 5520 gacgagaacg cgccctcctc gtgggccgcc cggctcgccc ggctgtccgc cgccgaccgc 5580 gaccgcgccc tcaacgaact cattcgcgag cagatcgcga ccgtcctggc acacccctca 5640 cccgacacca tcgaactggg ccgcgccttc caggagttgg gcttcgactc gctcaccgcc 5700 ctggaactcc gcaaccgcct ctccacggcc accggcatcc ggctgcccgc caccctcgtc 5760 ttcgaccacc cgagccccac cgccctcgta cgccatctcc acagccatct ccccgacgag 5820 gcccagcaca cgtccccgac cgcccccggc gcctctgcgg agggcaccgc cgccacggcc 5880 accggcatcg acgacgaccc gatcgccatc gtcggcatgg cgtgccgcta cccgggcggc 5940 gtgacctcgc ccgagcagct gtggcagctc gtggccaccg gcaccgacgc catcggcccg 6000 ttccccgagg accgcggctg ggacacggcc ggactgttcg atcccgaccc cgaccaggtc 6060 ggccacagct acacccgcga aggcggcttc ctctacgacg ccgcccgctt cgacgcgggc 6120 ttcttcggca tcagcccgcg cgaggccgcc gccaccgacc cgcagcagcg cctgctcctg 6180 gaaaccgcct ggcaggcgtt cgaacacgcg ggcatcgacc ccgccgccct gcgcggcacc 6240 ccgtgcggcg tcatcaccgg aatcatgtac gacgactacg gatcccgctt cctcgcgcgc 6300 aaaccggacg gcttcgaggg ccgcatcatg accggcagca cgccgagcgt ggcctccggc 6360 cgggtcgcgt acaccttcgg cctggagggc cccgccatca cggtggacac cgcgtgctcc 6420 tcctcgctgg tcgcgatgca cctggcggcg caggcgctgc ggcagggcga gtgcgaactg 6480 gccctggccg ggggtgtgac cgtgatggcc accccgaaca ccttcgtgga gttctcccgc 6540 cagcgcggcc tggcccccga cggccgctgc aagccgttcg ccgccgcggc ggacggcacc 6600 ggctggggcg agggcgccgg actcgtcgtc ctggagcgcc tctccgacgc gcgccgcaag 6660 ggacaccgcg tcctcgccct gctgcgcggt tcggccgtga accaggacgg cgcgagcaac 6720 ggcatgaccg ccccgaacgg tccctcgcag gaacgggtca tccgcaccgc cctggccggc 6780 gcgggccgtg gtcccgagga catcgacgtg gtggaggcgc acggcaccgg caccacgctc 6840 ggcgacccga tcgaggcgca ggccctgctc gccacgtacg ggcaggggcg cccggaggac 6900 cgcccgctct ggctcggctc ggtgaagtcg aacatcggcc acacgcaggc cgccgccggt 6960 gtcgcgggcg tcatcaagat ggtcatggca ctgcgccacg agcaactgcc cacgaccctg 7020 cacgccgacg agccgacccc ccacgtgcaa tgggacggcg gcggcgtacg tctcctgacc 7080 gaaccggtcc cgtggtcgcg cggcgagcgc acgcggcgcg ccggggtgtc gtccttcggg 7140 atctccggga cgaacgcgca cctgatcctg gaggagccgc cggaggagga cctgcccgag 7200 cccgtggcgg cggagccggg tggggtggtg ccgtgggtgg tgtccgggcg gacgccggac 7260 gcgttgcgtg aacaggcgcg gcggctcggc gagtttgtcg tcggtgccgg ggatgtgtcg 7320 gcagccgagg tgggatggtc actggccacg acgcggtcgg tgttcgagca ccgggccgtg 7380 gtggcgggcc gggaccggga cgatctggtt gccgggatgc aggcgctggc ggcaggggag 7440 acgccgacag atgtcgtgtc cggtgcggcg gcttcctccg gtgcggggcc ggtgttggtg 7500 ttcccggggc aggggtcgca gtgggtgggc atgggtgccc agctccttga cgagtccccc 7560 gtcttcgcgg cgcggatcgc ggagtgtgag caggcgctgt cggcgtacgt ggactggtcg 7620 ctgagtgatg tcctgcgcgg ggacgggagt gagctgtccc gggtcgaggt cgtgcagccc 7680 gtgttgtggg cggtaatggt ctcgctggct gccgtctggg cggattacgg ggtcactccg 7740 gccgctgtgg tggggcattc gcagggtgag atggctgccg cgtgtgtggc gggggcgctg 7800 tcgctggagg atgcggcgcg gattgtggcg gtacgcagtg acgcgcttcg tcagctgcaa 7860 gggcacggcg acatggcctc actcggcact ggtgccgagc aggccgctga gctgatcggt 7920 gatcggccgg gagtggtcgt cgcggcagtc aacgggccgt cgtctaccgt gatttcgggg 7980 ccgccggagc atgtggccgc tgtggtcgcg gaggcggagg cacgtggtct gcgcgcccgt 8040 gtgatcgacg tcgggtatgc ctcgcacggc ccccagatcg accagctcca cgacctcctc 8100 accgagggcc tggctgacat ccggcccgcg aacacggacg tggccttcta ttcgacggtc 8160 accgccgagc gcctgacgga caccacagcc ctggatacgg attactgggt gaccaacctc 8220 cgccagccgg tccggttcgc cgacaccatc gaagcgcttc tcgcggacgg ctatcgcctg 8280 ttcatcgagg ccagcgcgca cccggtgttg ggcctgggca tggaggagac catcgagcag 8340 gcggacatcc ctgccacggt cgtccccacc ctgcgccgcg accacggcga caccacccag 8400 ctcacccgcg ccgccgccca cgccttcacc gccggcgccg atgtcgactg gcgacgctgg 8460 ttcccggccg accccacccc ccgtaccgtc gacctcccca cctacgcctt ccagcaccag 8520 cactactggc tggaggagcc cagtgggctc accggagacg ccgccgacct cggcatggtg 8580 gccgccgggc atccgctgct cggtgcctgt gtggaactcg cggagagcga ctcgtacttg 8640 ttcaccgggc ggctctcgcg cagggctccg tcctggctgg ccgaacacgt ggtggcgggg 8700 acggttctgg tgccgggtgc ggcgttggtg gagtgggtgc tgcgggccgg cgatgaggcg 8760 ggatgcccga cgattgagga actgacgctc caggcgccgt tggtgctgcc cgagtcgggc 8820 gggttgcagg ttcaggtggt cgtgggtgcg accgatgagc agagcggccg tcgtgacgta 8880 cacgtgtatt cgaggtctga gcaggacgcg tcggcggtgt gggtgtgcca tgccgtcggt 8940 gtggtgagct ccgaaatgcc agaagcggca gccgagttga gtgggcagtg gcctcctgcc 9000 ggggccgaag ccgtggatgt cgaggacttc tacgcgcggg ccgcggaggc cggatacgcc 9060 tacggtccgg cgttccaggg gctgcgggcg ctgtggcggc acgggacgga gctgttcgcc 9120 gaggtggtgc tgcccgaaca ggcgggtggg cacgacggtt tcggcatcca cccggcgctg 9180 ctggacgccg ccctgcatcc gctgatgctc ctcgaccggc ccgcggacgg gcagatgtgg 9240 ctgccgttcg cgtggagcgg ggtgtcgctg aacgcggacc gggcgaccca cgtccgtgtc 9300 cggctctccc cgcgggggga ggcggccgag cgtgacctgc gggtcgtcat cgccgacgcg 9360 accggcgcgc ccgtcctgac ggtcgacgcc ctgaccctgc gcgcggccga tcccggccgg 9420 ctgggtgcgg cggcccgtgg cggtgtcgac ggcctctaca ccgtcgactg gaccccgctg 9480 cccctgcccc agccccttcc gctgccgcgg acggatgcag gggggagtgc cgactgggtc 9540 atactctcgg acaactccag tgcagctctg gctgatgccg tgtcgtccgc gacggcggca 9600 ggtggcggag cgccgtgggc attgctcgct cccgtgggtg gcggctctgc cgatgacggg 9660 ctgccggtgg tgcggcggac cctctccctc gtacaggagt tcctggccgc cccggagctg 9720 accgagtccc gtctcgtcat cgtgacacgc ggtgccgtgg ccaccgacgc cgatggtgac 9780 gtcgcggcgt ccgcggcagc ggtatggggc ctgatccgca gcgcccagtc ggagaacccg 9840 ggccgcttcg tcctgctcga cgtcgaggag gagcacctcc acccggacgg cggggaactg 9900 ccgtacgccg ccctgcgcca cgccgtagag gagctcgacg agcctcaact tgccctccgc 9960 agcggcaaat tcctcgtacc gcgcatgacg cccgccgccg cccccgagga gctcgtcccg 10020 ccggtcggta cgtccggctg gcgcctcggc acctccggta cggccaccct ggagaatctg 10080 tcggtgatcg acgctcccga ggcgttcgcg ccgctggagc ccgggcaggt gcggatctcc 10140 gtacgggcgg cgggcatgaa cttccgtgac gtgctgatcg cgttgggcat gtatcccgac 10200 aagggcacgt tcgcgggaag cgagggcgcc ggacatgtga cggaggtggg accgggcgtc 10260 actcatctgt cggtcggtga ccgggtgatg ggtctgttcg agggcgcgtt cgctccgctg 10320 gccgtcgcgg acgcccggat ggtcgtcccg attccggagg gctggagctt ccaggaggcc 10380 gcggcggtgc ccgtggtgtt cctcacggcc tggtacggcc tcgtggacct cggccgcctc 10440 cgggcgggcg aatcgctgct catccacgcg ggcaccggcg gagtgggcat ggccgccacc 10500 cagatcgccc gccacctggg cgccgaggtg ttcgccaccg cgagccccgc caagcacggc 10560 gtgctcgacg gcatgggcat cgacgcggcc caccgcgcct cctcccgtga cctcgacttc 10620 gaggagacct tgcgggcggc gacgggcggg cgcggcatgg acgtcgtact caacagtctg 10680 gccggggagt tcaccgacgc ctcgctgcgg ctgctcgccg agggcgggcg catggtggac 10740 atgggcaaga ccgacaagcg cgaccccgac cgggtcgcgg ccgagcacgc gggcgcgtgg 10800 taccgggcct tcgacctcgt gccgcacgcg gggcccgacc ggatcgggga aatgctggcg 10860 gagctgggcg agttgttcgc ctccggcgcc ctggcgccgc tgcccgtcca gacctggccg 10920 ctgggccggg cgcgtgaggc gttccggttc atgagccagg cgaagcacac cggcaagctg 10980 gtgctggaga tcccgcccgc cctcgatccg gacggcacgg tgctcatcac cggcggcacc 11040 ggggtcctcg ccgccgcggt ggccgagcat ctggtgaggg agtggggcgt acgacacctg 11100 ctgctggccg ggaggcgcgg ttccgaggcg cccgggagca gtgaactcgc cgaggaactg 11160 accgagttgg gggccgaggt gacctttgcc gcggccgatg tcagtgatcc ggacgccgtg 11220 gcggagctcg tcggcaagac cgatccggcg cacccgctga ccggtgtgat ccacgcggcc 11280 ggtgtgctgg acgacgccgt ggtcaccgca cagaccccgg agagcctcgc gcgggtgtgg 11340 gcggcgaagg cgacggccgc acacctgctg cacgaggcga cccgggaggc gcgcctcggt 11400 ctcttcctgg tgttctcctc ggcggcggcg acactcggca gtccgggaca ggccaactac 11460 gcggcggcca acgcctattg cgacgccctc gtccggcaac ggcgtgccga gggcctggcc 11520 ggtctctcga tcggctgggg tctgtggcag acggcgagcg gcatgaccgg acacctcggc 11580 gagacggacc tggcacgcat gaagcgcacc gggttcaccc cgctgaccac cgaaggtggc 11640 ttggccctcc tcgacgccgc ccgcgcccac ggccgcccgc acgtggtcgc ggtggacctc 11700 gacgcgcgcg ccgtcgccgc gcagcccgcc ccgtcccggc ccgcgctcct gcgcgccctg 11760 gccgcgggtg cgaccccggg ggcccgcacc gcccggcgca ccgcggccgc gggcagcgtc 11820 gccccggcgg gcggtctcgc cgaccggctc gccggcctgc cgcatcccga acggcgccgg 11880 ctgctgctcg acctcgtacg tggcaacgtc gccggcgtcc tcgggcacag cgaccacgac 11940 gccgtccgcc cggacacgtc gttcaaggag ctcggcttcg actccctgac cgccgtggaa 12000 ctgcgcaacc ggctggccgc cgccaccggc ctgaagctgc ccgcggcgct cgtcttcgac 12060 taccccgagt cggccaccct cgtcgaccac ctcctggagc gtctgtcgcc cgacggcgcg 12120 ccgccgcccg tcaaggacgc cgcggacccc gttctcaacg acctcggcag gatcgagtcc 12180 tccctggacg cgctcgccct cgacgcggac gcgcgcagcc gggtcaccag gcgtctgaac 12240 accctgctgt cgaagctgaa cggagccgcc accgccggct ccccggcgga cgtcacggac 12300 ctggacgcgc tggacgcgct ggacgacgtg tccgacgacg agatgttcga gttcatcgac 12360 cgagagctgt gacccccctg cccgccccgt cccccttccc cgcccccacg ttccccgtgc 12420 ccttcgctga tggagaagtg acgttcgatg tcgagtgctg aagagtcgag tcctgatgtg 12480 tccggcacgg gtgtgtccgg tacgggagag tccgctacgg gtacgtcgag tacggaagcc 12540 aagcttcggc agtatctgaa gcgggtcacg gtggacctcg gccaggcccg ccggcggctg 12600 cgcgaggtgg aggagcgggc ccaggagccg atcgccatcg tctccatggc gtgccgcttc 12660 cccggcgaca cccgcacgcc cgaggccctg tgggacctgg tcgccgaggg cggcgacgcc 12720 atcgacgact tccccaccaa tcgcggctgg gacctggaga gcctctacca ccccgacccc 12780 gaccaccccg gcaccagcta cgtccgacgc ggcgggttcc tgtacgacgc ccccgccttc 12840 gacgcgtcgt tcttcgggat cagcccgcgc gaagccctgg ccatggaccc gcagcagcgg 12900 gtgctcatgg agacggcctg gcagctcctg gagcgggccg gcatcgaccc ggcctcgctg 12960 aagctgagcg ccaccggcgt ctacatcggc gcgggcgtgc tcgggttcgg cggcgcgcag 13020 cccgacaaga cggtagaggg ccacctcctg accggcagcg cgctgagtgt cctgtccggc 13080 cgcatctcct tcacgctcgg cctcgagggc ccgtcggtca gtgtcgacac ggcgtgctcc 13140 tcctcgctgg tctccatgca cctggcggcc caggcgctgc ggcaggggga gtgcgatctc 13200 gcgctggccg gcggtgtcac cgtgatgtcg acgcccggcg cgttcaccga gttctcccgc 13260 cagggcgcgc tgtctccgga cggccgctcg aaggctttcg cggcctcggc cgacggcacc 13320 ggtttctcgg agggcgcggg actgctcctc ctggagcggc tctccgacgc gcgccgcaac 13380 ggccacaagg tgctcgcggt gatccgcggc tcggccgtca accaggacgg cgcgagcaac 13440 ggtctcaccg cccccaacgg cccctcccag gaacgcgtga tccgcgccgc cctcgccaac 13500 gcgggcctgg gcgccgccga ggtcgacgcg gtcgaggcac acggcaccgg cacgaagctc 13560 ggcgacccca tcgaggccgg tgcgctgctc gccacctacg gccgcgacag ggacgaggac 13620 cggccgctgt ggctgggctc ggtcaagtcg aacatcggtc acccgcaggg cgcagcaggc 13680 gtcgcgggcg tcatcaagat ggtgatggcg ctgcagcgcg aactgctccc cgccaccctg 13740 tacgtcgacg agcccacccc gcacgtcgac tggtcctcgg gctccgtcag gctcctcacc 13800 gaaccggtcc cgtggacccg cggcgagcgc ccgcgccgcg cgggcgtgtc cgccttcggc 13860 atgtccggga cgaacgccca cgtgatcctg gaggaggcac cgcccgagga ggcagcggcc 13920 gcggagacac cggcggaagg gacaggcgca gtcgtcccgt gggtcgtctc cggccggggc 13980 gaggaagcgc tgcgggccca ggccgcacag ctcgccgagc acgtgcgcga cgacgaccag 14040 cggccggcgt caccgctgga ggtggggtgg tcgctcgcca cgacacggtc ggtgttcgag 14100 aaccgggccg tcgtcgtcgg ggacgaccgc gacgcgctcc tcgacggcct ccggtcgctg 14160 gcggcaggtg aggcgtcgcc ggacgtggtg tccggggcgg tcggccccac ggggcccggg 14220 ccggtcatgg tgttccccgg ccagggcggc cagtgggtgg gcatgggggc ccggctcctc 14280 gacgagtccc cggtgttcgc ggcccggatc gccgagtgcg agcaggccct gtcggcgtac 14340 gtggactggt ccctgaccga cgtgctgcgc ggggacgggt cggagctggc ccggatcgac 14400 gtcgtccagc ccgtgctgtg ggccgtcatg gtcgcgctcg ccgccgtctg ggcggaccag 14460 ggaatcgaac ccgccgccgt cgtcggccac tcgcagggcg agatagccgc ggcgtgcgtc 14520 gtgggcgcca tctccctgga cgaggcggcc cgcatcgtcg ccgtacgcag tgtgctgctg 14580 cggcagctgt ccggacgcgg cggcatggcg tccctgggga tgggccagga gcaggccgcc 14640 gacctgatcg acggacaccc gggtgtggtc gtcgcggccg tcaacgggcc gtcgtccacc 14700 gtcatctcgg gcccgcccga gggcatcgcc gccgtcgtcg ccgacgccca ggagcggggc 14760 cttcgcgcca gggccgtcgc ctccgacgtc gcgggccacg gcccgcagct ggacgcgatc 14820 ctggaccagc tcacggaggg cctggccggc atccggcccg ccgcgaccga cgtcgcgttc 14880 tactccaccg tcaccgccgg gcacctcacc gacaccaccg aactcgacac cgcgtactgg 14940 gtgcggaacg tgcgccggac ggtgcgtttc gccgacacga tcgacgcgct gctcgcggac 15000 gggtaccgcc tgttcatcga ggtgagcccc caccccgtcc tcaacctcgc gctggaaggc 15060 ctcatcgaac gggcggccgt gcccgccacg gtcgtgccca ccctgcgccg cgaccacggc 15120 gacaccaccc agctcgcccg cgccgcggcc cacgccttcg ccgccggcgc ggacgtcgac 15180 tggcggcgct ggttcccggc cgaccccgcc ccccgtaccg tcgacctgcc cacctacgcc 15240 ttccagcgcc aggacttctg gccggccccc gccggcgggc ggtccggcga ccctgccggg 15300 ctcggcctcg ccgcctccgg acacccgctc ctgggcgcct ccgtgggcct cgcgagcggg 15360 gacgtacacc tgctgagcgg gcgggtgtcc cggcagtccg ccgcgtggct ggacgaccac 15420 gtcgtggcgg gccaggccct ggtgcccggc gcggcgcagg tggagtgggt gctgcgggcc 15480 ggcgacgacg cgggctgctc cgccctggag gagctgacgc tccagacgcc gctcgtgctg 15540 cccgacaccg gcggcctgcg gatccaggtc gtcgtcgaag cggccgacgc acacggccgg 15600 cgcgacgtcc ggctgttctc ccgccccgat gacgacgacg ccttcgcgtc gacgcacccc 15660 tggacctgcc acgccacggg cgtgctcgcc cccgccccga cggacggcac caacggaacg 15720 cgggacgccg ccgacaccct ggacggcgca tggcccccgg ccgacgccga acccgtcccc 15780 gccgacgacc tctacgcgca ggccgaccgc accggatacg gctacggccc cgccttccgg 15840 ggcgtacggg cgctgtggcg ccacggcaag gacgtcctgg ccgaggtgac gctgcccaag 15900 gaggccggcg acccggacgg cttcggtatc cacccggccc tcctcgacgc cgtcctgcaa 15960 cccgccgcac tgctgctgcc cccgaccgac gccgaacagg tctggctgcc gttcgcctgg 16020 aacgacgtgg cgctgcacgc cgtacgggcc accacggtcc gggtgcgcct caccccgctc 16080 ggcgagcgga tcgaccaggg gctgcgcatc accgtggccg acgccgtggg cgcgcccgtg 16140 ctcaccgtcc gcgacctgcg ctcgcgcccg accgacacag gccgcctcgc cgcggccgcg 16200 acccgcgacc ggcacgggct gttcgacctg gagtggatcg cgccggagaa cgcggcggag 16260 aacgcggcgg gtccggcccg ggacgcgtcc gaagggtggg tgacactcgg cgaggacgcc 16320 gcgagcctcg cggacctgct ggcgtccgtc gaggcgggcg ctccggcgcc gcagctcgtg 16380 gccgcccccg tcgaacccga ccggaccgac gacggcctgg cactcgccac ccacgtcctc 16440 gacctcgtac agacctggct cgcctcgccc ctgcacgact cccgcctggt cctggtgacg 16500 cgaggggcag tgacggatgc ggatgtggat gtggctgccg cggccgtttg gggtctggta 16560 cgcagcgccc agtcggagca ccccggccgc ttcacgctga tcgacctcgg ccccgacgac 16620 acgcttgccg cagccatgca ggcggcgcac ctggaagagc cgcaactggc ggtgcacggc 16680 ggcgagatac gagtgccgcg actggtccgc gccacgaccg acccgaccgc cccgaacggg 16740 acaccggagg ccgaccggac ggcggacccg tccgaaggac tccaccggaa cggtacggtt 16800 ctcatcaccg gcggcaccgg cgtactcggc cgactggtgg ccgaacacct ggtcacggag 16860 tggggcgtac gccacctgct gctcgcgagc cgacgcggcg accaggcgcc gggtagcgcc 16920 gaactccgcg cccgcctgag cgaattggga gcatcggtcg agatcgcccc ggccgatgtc 16980 ggcgacgcgg aagcggtcgc cgcactgatc gcgtcggtcg acccggcgca cccgctcacc 17040 ggtgtgatcc acgcggccgg tgtcctggac gacgccgtga tcaccgccca gacccccgag 17100 agcctcgcgc gggtgtgggc gacgaaggcg acggcggccc gccatctgca cgaggcgaca 17160 cgggagacac ccctcgactt cttcgtggtg ttctcctcgg cggccgcctc gctcggcagc 17220 cccggccagg ccaactacgc ggcggccaac gcctattgcg acgccctcgt ccagcaccgc 17280 cgcgcccaag ggctcgcggg cctctcgatc gcctggggcc tgtggcaggc gaccagcggc 17340 atgaccgggc agctgagcga gaccgacctg gcgcgcatga agcgcaccgg gttcgccgcg 17400 ctgaccgacg agggcggcct ggccctgctc gacgccgccc gtgcccacga ccgggcctac 17460 gtggtcgcgg ccgacctcga cccgcgcgcc gtgaccgatg gcctgtcccc gctcctgcgc 17520 gccctcacgg cgcccgccac gcggcggcgc gtggcctccg aaggcctcgc cgacggggcg 17580 ctcgcgaccc gcctggccgg cctcgacgcg gacggccgcc taaggctcct caccgatgtc 17640 gtacgcgagt acgtcgcggc cgtcctcggc catggttccg ccgcccgggt gggcgtcgac 17700 atcgccttca aggacctggg tttcgactcg ctgaccgcgg tggagctgcg caaccggctg 17760 tcggccgcct gtgacgtgcg gctgcccgcc acactgatct tcgaccaccc caccccgcag 17820 gctctcgcca cccacctggt ggaccgcttg gcgggcagca cctccgcgac cacgacggtg 17880 aatgcgacgg cgccggcagc cgcccacgtc gccgcagggg ccgacgtcga cgcagacacc 17940 gacgacccgg tcgccatcgt cgccatgacg tgccggttcc cgggcggcgt cgcgtccccg 18000 gacgacctgt gggacctgct cgacgcacgc aaggacgcga tgggcgcctt ccccaccgac 18060 cgcggctggg acctggaacg cctcttccac cccgacccgg accaccccgg caccagctac 18120 accgaccagg gcggatttct tcccgacgcg ggtgatttcg atgcggcgtt cttcgggatc 18180 aatccgcggg aggcgctggc gatggatccg cagcagcggt tgttgctgga ggcgtcgtgg 18240 gaggtgttgg agcgtgcggg tatcgatccg acgacgctca agggcacccc gaccggcacc 18300 tacgtgggcc tcatgtacca cgactacgcc aagtccttcc ccacggccga cgcccagttg 18360 gagggctact cctacttggc gagcaccggc agcatggtct ccggccgcgt cgcctacacc 18420 ctgggccttg aaggtccggc ggtgacggtc gacaccgcgt gctcctcctc cctggtctcc 18480 atccacctgg cgacgcaggc actccggcac ggcgagtgcg acctcgccct ggcaggcggt 18540 gtgaccgtca tggccgaccc ggacatgttc gcgggcttct cgcgccagcg cggcctctca 18600 cctgacggcc gctgcaaggc ctacgccgcc gcggccgacg gagtcggatt ctccgaggga 18660 gtgggcgtat tgctccttga gcggttgtcg gatgcgcggc gtcatgggcg tcgggtgttg 18720 ggtgtggtgc ggggttcggc ggtgaatcag gacggtgcga gtaatgggtt gacggcgccg 18780 aatggtccgt cgcaggagcg ggtgattcgt caggcgttgg ccagtggtgg gttgtcgtcg 18840 gtggatgttg atgtggtgga ggggcatggg acggggacca cgttgggtga tccgatcgag 18900 gcgcaggctc tgctggccac atatgggcag gggcgtccgg aggaccgtcc gttgtggttg 18960 gggtcggtga agtcgaacat tggtcatacg caggcggctg cgggtgttgc gggtgtcatc 19020 aagatggtga tggcgatgcg gcatggtgtg gtgccggcga gtttgcatgt ggatgtgccg 19080 tcgccgcatg tggagtggga ttcgggtgcg gtgcggttgg cggttgagtc ggtgccatgg 19140 ccgcaggtgg agggtcgtcc gcgtcgggcg ggtgtgtcgt cgttcggcgc ttcggggacg 19200 aatgcgcacg tgatcgtgga gtctgttccc gatgggctgg aggaggactc ggtatcggtc 19260 ggcggtgagg ctcttgagac ggagactgac gggcgcttgg tgccgtgggt ggtgtcggcc 19320 cgcagcccgc aggccctgcg cgaccaggca ctacgcctgc gtgactttgc cagtgacgcg 19380 tcgttccgcg cgccgctcgc cgacgtgggc tggtcgctgc tgaagacgcg tgcgctgcat 19440 gagcatcgcg ccgttgtggt gggcgcggag cgggcagagc tgatcgccgc tctggaggcg 19500 ctggcgacgg gtgagccgca tgcggcgctg gtcggcccgg cttgctcgca ggctcgggtg 19560 ggtggcgatg acgtggtgtg gctgttcagt ggtcagggca gtcagttggt cggtatgggt 19620 gctggtttgt atgagcggtt cccggtgttt gcggctgcgt ttgatgaggt gtgcggcctg 19680 ttggaggggc cgttgggcgt ggaggcgggt gggttgcggg aggtggtgtt ccgtggcccg 19740 cgggagcggt tggatcacac ggtgtgggcg caggcggggt tgtttgcgct gcaggtgggg 19800 ttggcccggt tgtgggagtc ggtcggggtg cggccggatg tggtgctcgg gcattcgatc 19860 ggtgagatcg cggccgcgca tgtggcgggg gtttttgatc tggcggatgc gtgtcgggtg 19920 gtgggtgcgc gggcgcgttt gatgggtggg ctgcctgagg gtggggcgat gtgcgcggtg 19980 caggccacgc ccgccgagct ggccgccgac gtggacggat cggctgtaag tgtggcggca 20040 gtcaacaccc ccgactccac ggtgatttcg ggcccgtcgg acgaggtgga ccggattgct 20100 ggggtgtggc gggagcgtgg gcgcaagacg aaggcgctga gcgtcagtca tgccttccat 20160 tcggcgttga tggagccgat gctcgcggag ttcaccgaag cgatacgagg ggtcaagttc 20220 aggcagccgt cgatcccgct catgagcaat gtctccggag agcgggccgg cgaggagatc 20280 acggatccgg agtactgggc gaggcatgta cgtaatgcgg tgctcttcca gcccgccatc 20340 gcccaagtag cggattcagc gggcgtgttt gtggagctcg gccccgcgcc tgtgctgacc 20400 acggccgccc agcacaccct ggacgagtcg gacagccagg agtcggtgct ggtcgcgtct 20460 ctcgccggtg agcgtcctga ggagtcggcg tttgtggagg cgatggctcg tctgcatacc 20520 gctggtgttg ctgtggactg gtcggtgttg ttcgcgggtg atcgtgtgcc tgggctggtg 20580 gagttgccga cgtatgcgtt ccagcgggag cggttctggt tgagtggccg ttctgggggt 20640 ggggatgcgg cgactttggg gttggtggcg gcggggcatc cgttgttggg tgcggcggtg 20700 gagttcgcgg accggggtgg gtgtctgctg accggtcgtc tgtcgcggtc tggggtgtcg 20760 tggcttgctg atcatgtggt ggcgggtgcg gttttggtgc cgggtgctgc gttggtggag 20820 tgggcgttgc gggccggtga tgaggtcggt tgtgtgacgg tggaggagtt gatgttgcag 20880 gcgcctttgg tggtgcctga ggcgtcgggt ctgcgggttc aggtggtggt tgaggaggcg 20940 ggtgaggacg ggcggcgcgg tgttcagatc tacagccggc ccgacgcgga cgccgtgggc 21000 ggcgatgact cgtggatctg ccacgcgacc ggcgtactgt cacccgaaag cgctcgtctg 21060 gacacggagt tgggtggcgt ctggccaccg gccggtgccg aaccgctgga tgtcgacggc 21120 ttctacgcgc aggccggtga ggccgggtac ggatacggtc cggcgttccg ggggctgcgt 21180 gccgtgtggc ggcacggcca ggacctgctg gccgaggtcg tcctgcccga agccgccggt 21240 gcccatgacg gctacgggat ccaccccgcc ctcctcgacg ccaccctcca tccgctgctc 21300 gccgcccgct tcatggacgg ttccgaggac gatcagctct acgtaccgtt cgggtgggcc 21360 ggagtgtctc tgcgggcggt gggagccacg actgtgcgcg tgcgcctccg tccggtcggg 21420 gagagcgtcg accaagggct gagcgtgacg gtcaccgatg cgaccggcgg tcccgttctg 21480 agcgtcgact ccctccagac ccgccccgtg aagccgagcc aattggctgc ggcccaacag 21540 ccggacgtac gcggtctgtt cactgtggag tggacgccgc tgccgcagac ggatgccgac 21600 ggggaggccg actgggttgt gctctcggac ggtgttggcc gtctggctga tgtggtgtcg 21660 gcggcgggtg gtgaagcgcc gtgggcagtg gtcgctcctg tcgatgcgtc tgtgggcgac 21720 ggccgtgagg gtcttgacgg tcggctggtc gtggagcggg tgctgtcact cgtacaggag 21780 ttcctggccc tgccggagct ggccgagtcc cgtctcctcg tggtgacgcg cggtgcggtg 21840 gccaccggcg tcgacggtga cggtgacgtg gacgcgtccg ccgcagctgt atggggcctg 21900 gtccgcagtg ctcagtccga gaatccgggc cgcttcatcc tgctcgacgt ggacggcgac 21960 ggcgacgacc agggcccgga cctgaacggc cggcatctgc cccacgccac cctgcgtcac 22020 gccgccgagg aactcgacga gccccaactc gccctgcggg aagggacgct ctacgtcccc 22080 cgactgaccc aggcgcgcca gtccgccgaa ctcgtcgtgc cgcccggtga accggcgtgg 22140 cgcctgcgga tggtgcacga cggctcgctg gacgccctgg cggcagtggc ctgcccggag 22200 gccctggagc ccttggcgcc ggggcaggtg cgtatcgccg tacacgccgc gggcatcaac 22260 ttccgtgacg tactggtggc cttgggtatg gtccccgcgt acggggccat gggtggcgaa 22320 ggtgccggtg tcgtgacgga ggtcggtccc gaggtcaccc atgtctcggt gggcgaccgc 22380 gtgatgggcg tgttcgaggg cgcgttcggc cctgtggtga tcgccgaggc gcggatggtc 22440 acacctgtcc cgcagggctg ggacatgcgg gaggcggccg gtattccggc ggccttcctg 22500 acggcttggt acgggttggt ggagctggcc ggtctgaagg cgggcgagcg ggtgctggtc 22560 catgccgcga cgggtggtgt ggggatggcg gcggtgcaga tcgcccggca tgtgggtgcc 22620 gaggtgttcg ccaccgcgag tccgggcaag cacgccgtgc tggaggagat gggcatcgac 22680 gccgcccacc gcgcctcctc ccgggacctc gccttcgagg gcacgttcag ggaagcaacg 22740 ggcggccgcg gcatggacgt cgtgctcaac agccttgccg gcgagttcat cgacgcctct 22800 ctgcggttgc tcggcgacgg cggccggttc ctggagatgg gcaagaccga tgtgcgggcc 22860 gccgaagagg tggctgcgga gcacgcggac gtctcgtaca cggcgtacga cctcgtcggt 22920 gatgccggac ccgaccgcat cagcaacatg ctggacaagc tcgtcgaatt gttcgcctca 22980 gaacggctta agccgctgcc ggtacgttcc tggccgctgg acaaggcgca ggaggcgttc 23040 cggttcatga gtcaggcgaa gcacaccggc aagctggtgc ttgagatccc gcctgccctc 23100 gaccccgagg gcacggttct ggtcaccggg ggcaccggtg cgctggggca ggtcgtggcc 23160 gagcatctgg tccgggagtg gggcgtacgg cacctgctgc tggccagccg tcgcggtccg 23220 gaggcgccgg gcagcgacga actggcctcg aagctcaccg ggttgggtgc cgaggtcacc 23280 attgtcgcgg ccgatgtcag cgacccggcc tcggtggtgg agctggtcgg caagacggat 23340 ccctcgcatc cgttgacggg tgtcgtgcac gcggcgggcg tgttggagga cggtgtcgtg 23400 accgctcaga cgcctgaggg gctggcgcgg gtgtgggcgg ccaaggctgc tgcggcggcg 23460 aatctccatg aggcgacccg ggagatgcgt ctcggcctgt tcgtggtgtt ctcctcggcg 23520 gccgccacgc tcggcagtcc gggccaggcc aactacgcgg ccgccaatgc ctattgcgac 23580 gcgctgatgc agcaccgacg ggcggtgggc caggtcggcc tgtcggtcgg ctggggtctc 23640 tgggaggcgc cggacgccaa gccgggtgtt gccgccgacg ccaaggcgag tgctgccacc 23700 gtcggcaagg cgagtgctct atccgacggc acgaacggca gcgctcccca ggacacgacc 23760 ggcaccgccc cccagggcat gaccggcgga ctcaccgaca ccgacgtagc ccgcatggca 23820 cgtatcggcg tcaagggcat gagcaacgcc cacggtctcg ccctgttcga cgccgcgcac 23880 cgccacggcc gcccccacct ggtcggcttc aacctcgacc tgcgcaccct ggccacgcac 23940 cccctgcaca cccggcccgc ccttctgcgc ggcctggcca cccccaccgc cggcggggcg 24000 agcaggccga ccgcgacggc gggcggacag cccgccgacc tggcgggccg gctggccgcg 24060 ctgtcgccgt cggaccggca ccacacgctg gtccggctca tcagggaaca ggccgccacc 24120 gtgctcgggc accacccgga cagtctcacc acgggcagca ccttcaagga actcggattc 24180 gactccctga ccgcggtcga actgcgcaac aggctgtccg ccgccaccgg tctccggctc 24240 cccgccggcc tggtcttcga ccacccggac gccgacatcc tggccgaaca cctcggcgcg 24300 caactcgccc ccgacgggga cacccccgcc ggtgcggaag ccaccgaccc ggtcctccgc 24360 gacctggcga aactcgagaa cgccctctcc tccaccctcg tcgagcacct cgacgccgac 24420 gcggtcacgg cccgactgga agcactcctg tcgaactgga aggcggcgag cgcggcgccc 24480 ggctcgggca gcacgaagga gcagctccag gttgccacga ccgaccaggt cctcgacttc 24540 atcgacaaag aactgggtgt gtgaaacgac cgtgcacggc gcgacaacca cgctgaaggc 24600 tgggtgaact ctcatggcga gtgaagagga actggtcgac tacctcaagc gggtcgccgc 24660 cgaactgcac gacacccggc agcgcctgcg cgaggtcgag gaccggcggc aggagccggt 24720 ggccgtcgtc ggcatggcct gccgtttccc cggcggcatc gagacgcccg agggactgtg 24780 ggagctggtc gcggccggcg acgacgccat tgagcccttc cccaccgacc ggggctggga 24840 cctggaaggc atctaccacc cggaccccga ccacccgggt acctgctacg tccgggaggg 24900 cgggttccta gccgcccctg accggttcga ctccgacttc ttcggcttca gcccgcgcga 24960 ggccctggcc agcagcccgc aactgcgact gctcctggag acgtcctggg aggccctcga 25020 acgggcgggc atcaaccccg cctcgctcaa gggcagcccc accggcgtct acgtcggcgc 25080 cgcgaccacc ggcaaccaga cgcagggcga ccccggcggc aaggcgaccg agggttacgc 25140 gggcaccgcg cccagcgtcc tctcgggccg cctctcgttc acgctcggcc tggagggccc 25200 ggcggtgacc gtcgagacag cgtgctcctc ctcgctggtg gcgatgcacc tggcggccaa 25260 cgccctgcgc cagggcgagt gcgacctcgc cctcgcgggc ggcgtcaccg tcatgtccac 25320 ccccgaggtg ttcacaggct tctcgcgtca gcggggactg gcccccgacg gccgctgcaa 25380 gccgttcgcc gccgcggccg acggcacggg ctggggcgag ggcgcgggcc tgatcctcct 25440 ggagcgcctc tccgacgccc gcaggaaggg ccacaaggtc ctcgcggtga tccggggctc 25500 ggcgatcaac caggacggcg cgagcaacgg cttcaccgcg cccaacggcc cctcgcagcg 25560 ccgcgtcatc cgccaggcac tctccagcgc ccacctctcc acgtcggaga tcgacgtcgt 25620 cgaggcgcac ggcaccggca ccaggctcgg cgaccccatc gaggccgagg cgctcatcgc 25680 cacctacggc aaggagcgcg aggacgaccg tcccctgtgg ctcggctcgg tcaagtccaa 25740 catcggccac acgcaggccg ccgcgggcgt cgccggagtc atcaagatgg tgatggcgct 25800 acagcgcgaa ctgcttcccg ccaccctgaa cgtcgacgag ccgaccccgc acgtccagtg 25860 ggagggcggc ggcgtacgcc tcctgaccga accggtcccg tggtcgcgcg gcgaacgccc 25920 gcgccgcgcc ggaatctcct ccttcggcat atcgggcacg aacgcgcacg tggtcctgga 25980 ggaggcgccg ccggaggagg acgtgccggg ccccgtggct gcggagccgg aaggggtggt 26040 gccgtgggtg gtctccgcgc ggaccgagga ggcgttgagc gaacaggcgc ggcgcctggg 26100 cgagttcgtg gccgacacgg acccgtcgac cgctgacgtc gggtggtcac tgaccacgag 26160 cagggcgatc cttgaacacc gcgctgtggt ggtggggcgt gatcgggatg cgctgacggc 26220 cggcctggcg gcgttggccg cgggtgagga gtcggcggat gtggtggctg gggtggccgg 26280 tgatgtgggt cctgggccgg tgttggtgtt tccggggcag gggtcgcagt gggtgggcat 26340 gggcgcccag ctccttgacg agtcgcccgt cttcgcggcg cggatcgcgg agtgtgagca 26400 ggcgctgtcg gcgtacgtgg actggtcgct gagtgcggtg ttgcgcgggg atgggagtga 26460 actgtcccgg gtcgaggtcg tgcagccggt gttgtgggcg gtgatggtct cgctggctgc 26520 cgtctgggcg gattacgggg tcaccccggc cgctgtgatc gggcactcgc agggcgagat 26580 ggccgccgcg tgcgtggcgg gggcgctgtc tttggaggat gcggcgcgcg tcgtggccgt 26640 acgcagtgac gcgcttcgtc agctgatggg gcagggcgac atggcgtcgt tgggcgccag 26700 ctcggagcag gcggctgagc tcatcggtga tcggccgggc gtatgcatcg cagcggtcaa 26760 cgggccgtcc tcgacagtca tttcaggacc gccggagcat gtggcagccg tggtcgcgga 26820 tgcggaggaa cgtggtctgc gcgcccgtgt catcgatgtc ggctatgcct cgcacggtcc 26880 ccagatcgat cagctccacg acctcctcac cgaccggctc gccgacatcc ggcccgcgac 26940 cacggacgtg gccttctatt cgacggtcac cgccgagcgc ctgacggaca ccacggccct 27000 ggatacggat tactgggtta ccaacctccg ccagccggtc cgtttcgccg acaccatcga 27060 tgcgcttctc gcggacggct atcgcctgtt catcgaggcc agcgcgcacc cggtgctggg 27120 tctgggcatg gaggagacca tcgagcaggc ggacatcccc gccacggtcg tccccaccct 27180 gcgccgcgat cacggtgaca ccacccagct cacccgtgcc gcagcgcacg ccttcaccgc 27240 cggcgccacc gtcgactggc ggcgctggtt cccggccgac cccacccccc gcacgatcga 27300 cctgcccacc tacgccttcc agcgccgcag ctactggttg ccggtggacg gtgtcggaga 27360 tgtgcggtcg gccgggctgc ggcgggtgga acactcgctg ttgcccgcgg cgctcggtct 27420 cgccgatggt gcgctcgtgc tgaccggacg gctcgcggcg tccggtggtg gtggcggttg 27480 gctcgcggat cacgcggtgg cgggcacgac gctcgtcccc ggtgccgcgc tggtcgagtg 27540 ggcgttgcgg gccgccgacg aggcgggctg cccctccctt gaggagctga cgctccaggc 27600 acctctggtg ctgcccggct ccgggggcct ccaggtccaa gtggtcgtgg gtccggccga 27660 cggacagggc ggccggcgtg aggtgcgcgt cttctcgcgt gtcgactcgg acgacgaggc 27720 agcggggcag gacgaggggt ggtcgtgtca cgcgaccggt gtgctgagcc ccgagcccgg 27780 tgcggtaccg gacgggctca gcggacagtg gcccccgacg ggcgccgagc cgctggagat 27840 cagtgatctc tacgagcagg cggcatcggc gggatacgag tacgggccgt cgttccgggg 27900 cctgcgctcc gtgtggcggc acgggcataa cctgctggca gaggtggagc tgcccgaaca 27960 ggcaggtgcg cacgacgact tcggcatcca ccccgtactg ctggacgccg cgctgcaccc 28020 ggcgctgctg ctcgaccaga acgcgcccgg cgaagagcaa gagccagccc agcccgctct 28080 tcgcctgccg ttcgtgtgga acggcgtctc cctgtgggcc accggcgccg cgaccgtgcg 28140 ggtacggctg gccccgcacg ggggagggga gacggacgat agcgccgggc tgcgcgtgac 28200 ggtcgccgac gccaccggag caccggtgct gagcgtggac tccctcgctc tgcgccccgc 28260 tgaccccgaa ctgctgcgca cggccggtcg ggcgggcagc ggcaccaacg gcttgttcac 28320 ggtggagtgg accgctctgc ccccggcgga cgtggccgac cacgccgcag gcgacggctg 28380 ggcggtgctc ggtcaggacg tacccgactg ggccggagcg gacatgcccc ggcatcccga 28440 catggcctcc ctgtcggccg cgctggacga gggaacgcag gcccctgcgg ccgtcttcgt 28500 ggagaccaca gccacatcgc acgccacacc gaacaccgca gcggacgtga cgctcgacgc 28560 gtccggccgg gcggtcgccg agcgcaccct gcacctgctg cgggactggc tcgccgaacc 28620 gcgcctcgcc gagacccggc tcgtcctcat cacccaccac gcggtgacga ccccggcgga 28680 cgacgacgtg aacgccgcac ccctcgacgt cccggccgcc gccctgtggg gactgatccg 28740 cagcgcacag gccgaacacc cggaccgctt cgttctgttg gacaccgacg cgaaggccaa 28800 caccgacccc ggccccgaca ccagtactga ccacagcacc gcatcgggta cgtaccgaac 28860 cgtcatcgcg cgggccctcg ccaccgggga gccacagctg gccgtgcgcg cgggagaact 28920 gctggctccc cgcctcgccc gagccgccac ccccacaccc gagaccccca cacccgagac 28980 acagcccgac accggatccg ggtccgaggc cggggccggg tccggatctg gacccggcgc 29040 gacactggac cccgacggca ccgtcctcat cgcgggcggc accggcatga tgggtggtct 29100 cgtcgccgaa cacctggtcc gcgcctggtc ggtgcggcac ctcctgctcg tcagccggca 29160 agggcccgac gcgccggacg cccgcgacct cgccgaccgg ctggtcggcc tgggcgcgac 29220 ggtacggatc gtcgcggccg acctgacgga cgggcgggcc accgcggacc tcgtcgcgtc 29280 ggtcgacccg gcgcacccgc tcaccggtgt gatccacgcg gccggcgtcc tggacgacgc 29340 cgtggtcacc gcgcagacct ccgaccagct ggccagggtg tgggcggcca aggcgtccgt 29400 cgccgccaac ctggacgcgg ccacgtcgga gctgccgctc ggcttgttcc tgatgttctc 29460 gtccgccgcc ggtgtcctcg gcaacgcggg ccaggccggt tacgcggccg ccaacgcctt 29520 cgtcgacgcc ctggtcggcc gccgtcgcgc caccggcctg cccggcctgt cgatcgcctg 29580 gggcctgtgg gcgcgcggca gcgccatgac ccggcacctg gacgacgccg acctcgcgcg 29640 gctgcgtgcc ggcggggtca agcccctgct ggacgagcag ggcctcgccc tcctcgacgc 29700 ggcgcgcgcc accgccgcgc acacctcgct ggtggtcgcg gccggtatcg acgtacgcgg 29760 actgaacagg gacgacgtcc ccgcgatcct ccgcgacctg gcgggccgga cccgccgcag 29820 ggcggccgcc gactccaccg tcgaccaggc cgcgctggag cggcgcctca cgggcctgga 29880 cgaggccgag cgccgggctg tcgtcaccga cgtcgtacgc gaatgcgtgg cggccgtgct 29940 cggccaccgg tcggcggccg acgtacgcac cgaggccaac ttcaaggacc tcggcttcga 30000 3 30000 DNA Streptomyces cinnamonensis Nucleotides 60001 - 90000 of the monensin biosynthetic gene cluster 3 ctcgctcact gcggtgcagc tgcgcaaccg cctctcggcg gcgagcggcc tccgcctgcc 60 cgccaccctg gccttcgacc accccacccc ccaggcgctg gcggcgtacc tcggcacgcg 120 cctgagcggc cggaccgcca cccccgtcgc acccgtggcg ccttccgcgg ccgcgacgga 180 cgagccggtg gcgatcgtcg cgatggcctg caagtacccg ggtggagcga cctcgccgga 240 aggcctctgg gacctggtcg cggagggcgt ggacgcggtc ggcgccttcc cgacgggccg 300 cggctgggac ctcgaacggc tcttccaccc cgacccggac caccccggca cgagttacgc 360 cgacgaaggg gccttccttc ctgacgcggg cgatttcgat gcggcgttct tcgggatcaa 420 tccgcgggag gcgctggcga tggatccgca gcagcggctg ttgctggagg cgtcgtggga 480 ggtgttggag cgtgcgggta tcgacccgac gacgctcaag ggcaccccga ccggcacgta 540 cgtcggcgtg atgtaccacg actacgcggc aggcctcgcc caggacgccc aactggaggg 600 ctactccatg ctcgccggct ccggcagcgt ggtgtccggc cgcgtcgcct acaccctggg 660 gcttgagggt cctgcggtga cggtcgacac cgcgtgctcc tcgtccctgg tctccatcca 720 cctggccgcg caagcactgc gacagggcga gtgcactctc gccctcgcgg gcggcgtgac 780 cgtcatggcc acgcccgagg tgttcaccgg attctcgcgc cagcgcggcc tggcccccga 840 cggccgctgc aagccgttcg ccgccgccgc cgacggcacc ggctggggcg agggtgtcgg 900 tgtgttgttg ctcgagcggt tgtcggatgc gcggcgtcat gggcgtcggg tgttgggtgt 960 ggtgcggggt tcggcggtga atcaggacgg tgcgagtaat gggttgacgg cgccgaatgg 1020 tccgtcgcag gagcgggtga ttcgtcaggc gttggccagt ggtgggttgt cgtcggtgga 1080 tgttgatgtg gtggaggggc atgggacggg gaccacgttg ggtgatccga tcgaggcgca 1140 ggctctgctg gccacgtatg ggcaggggcg tccggtggat cgtccgttgt ggttggggtc 1200 ggtgaagtcg aatattggtc atacgcaggc ggctgcgggt gttgcgggtg tcatcaagat 1260 ggtgatggcg atgcggcatg gtgtggtgcc ggcgagtttg catgtggatg tgccgtcgcc 1320 gcatgtggag tgggattcgg gtgcggtgcg gttggcggtt gagtcggtgc catggccgga 1380 ggtggagggt cgtccgcgtc gggcgggtgt gtcgtcgttc ggggcttcgg gaacgaatgc 1440 gcacgtgatc gtggagtctg tgcccgatgg gctgggggag gactcggtat cggtcagtgg 1500 tgaggctccc gagactgaga ctgacgggcg cttggtgccg tgggtggtat cggcccgcag 1560 cccgcaggcc ctgcgcgacc aggcactacg cctgcgtgat gcggtggcgg ccgactcaac 1620 ggtgtcggtg caggatgtgg gctggtcgct gctgaagacg cgtgcgctgt tcgagcagcg 1680 ggcggtggtg gtggggcgtg agagggctga actcctgtcg gggcttgctg tgttggccgc 1740 tggcgaggag cacccggctg tgacgcggtc ccgtgaggac ggggttgctg cgagcggtgc 1800 tgtggtgtgg ctgttcagtg gtcagggcag tcagttggtc ggtatgggtg ctggtttgta 1860 tgagcggttc ccggtgtttg cggctgcgtt tgatgaggtg tgcggcctgt tggaggggcc 1920 gttgggcgtg gaggcgggtg ggttgcggga ggtggtgttc cgtggcccga gggagcggtt 1980 ggatcacacg atgtgggcgc aggcggggtt gtttgcgctg caggtggggt tggcccggtt 2040 gtgggagtcg gtcggggtgc ggccggatgt ggtgctcggg cattcgatcg gtgagatcgc 2100 ggccgcgcat gtggcggggg tctttgatct ggcggatgcc tgtcgggtgg tgggggcgcg 2160 ggcccgtttg atgggtgggc tgcctgaggg cggggcgatg tgcgcggtgc aggccacgcc 2220 cgccgagctg gccgccgacg tggacgactc tggtgtgagt gtggcggcgg tcaacacacc 2280 tgattcgacg gtgatttcag ggccgtctgg tgaggtggat cggattgctg gggtgtggcg 2340 ggagcgtggg cgtaagacga aggcgctgag cgtcagtcat gccttccact cggcgttgat 2400 ggagccgatg ctcgcggagt tcaccgaagc gatacgagag gtcaagttca cgcggccgaa 2460 ggtgtcgttg atcagcaacg tctctggtct ggaggcgggt gaggagatcg cgtccccgga 2520 gtactgggca cgccatgtac gccagacagt gctcttccag cccggcatcg cccaagtggc 2580 ttccacggca ggcgtgtttg tcgagctcgg ccccggcccc gtactgacta ctgccgccca 2640 gcacaccctg gacgacgtaa ccgataggca tggccccgaa ccggtactgg tgtcctcgct 2700 ggccggtgag cgtcctgagg agtcggcgtt cgtggaggcg atggctcgtc tgcataccgc 2760 tggtgttgct gtggactggt cggtgttgtt cgcgggtgat cgtgtgcctg ggctggtgga 2820 gttgccgacg tatgcgttcc agcgggagcg gttctggttg agcggccgtt ctgggggtgg 2880 ggatgcggcg actttgggtc tggtggcggc ggggcatccg ttgttgggtg cggcggtgga 2940 gttcgcggac cggggtgggt gtctgctgac cggtcggctg tcgcggtctg gggtgtcgtg 3000 gcttgctgat catgtggtgg cgggtgcggt tttggtgccg ggtgctgcgt tggtggagtg 3060 ggcgttgcgg gccggtgatg aggtcggttg tgtgacggtg gaggagttga tgttgcaggc 3120 gcctttggtg gtgcctgagg cgtcgggtct gcgggttcag gtggtggtcg aggaggcggg 3180 tgaggacggg cggcgcggtg tccagatcta tagccggcct gacgcggacg ccgtgagcgg 3240 cgacgactcg tggatctgcc acgcgaccgg caccctcacc ccccagcaca ccgacgctcc 3300 gaacgacgga ctggccggcg cgtggcccgc ggcgggcgcc gtgccggtgg acctggcggg 3360 cttctacgag cgcgtggcgg acgcgggcta tgcgtacggc ccggggttcc aggggctgcg 3420 tgccgtgtgg cggcacggtc aggacctgct ggccgaggtc gtcctgcccg aagccgcggg 3480 tgcccatgac ggctacggca tccaccccgc cctcctcgac gccaccctcc acccggccct 3540 gctcctcgac tggcccgggg aggtgcagga cgacgacggg aaggtctggc tgcctttcac 3600 ctggaaccag gtctccttgc gggctgcggg agccgccacc gtacgcgtac gtctctcgcc 3660 cggcgagcac gacgaggcgg aacgggaagt acaggtactg gtggccgacg ccaccgggac 3720 cgacgtcctg agcgtggggt cggtgacgtt gcgtcccgcc gacatccggc aactgcaggc 3780 cgtgccgggt cacgacgacg gtctgttctc ggtggactgg acgccgctgc cgctgtcgcg 3840 gacggatgtg tcgcagacgg atgccgacgg ggatgccgac tgggttgtgc tctcggacgg 3900 tgtcggcagc ctggctgatg tggtgtcggc ggcgggtggt gaagcgccgt gggcagtggt 3960 cgctcccgtc ggtgcatccg cgggcggcgg ccttgccggc tttgaccgcc gtgagggtct 4020 tgacggtcgg ctggtcgtgg agcgggtgtt gtcactcgta caggagttcc tggccgcgcc 4080 ggagctggcc gagtcccggc tcctcgtgct gacccgcggc gccgtggcga ccggcggcga 4140 cggcgacggt gatgtggacg cgtccgccgc agccgtatgg ggcctggtcc gcagtgctca 4200 gtccgagaac ccgggccgct tcatcctgct cgacgtggac atggacgtgg acgtcgacgt 4260 ggacatggac gtggacgtcg acgtggacgt cgacgtggac gtggacggag acggcaatgg 4320 cagcgacctg gacccggacc tgaacggccg acgacttccc cacgccaccc tgcgtcacgc 4380 cgccgaggaa ctcgacgagc cccaactcgc cctgcgcgac ggacaactgc tcgttccgcg 4440 gctggtccgc gccaccggcg gcggactcgt cgtggcgccc accgaccgtg cctggcgcct 4500 ggacaaggga agcgccgaga cgctggagag cgtcgcgccg gtcgcgtacc ccggagtcat 4560 ggaacccctg ggccccggcc aggtccgcct cggcatccac gccgcgggca tcaacttccg 4620 cgacgtcctg gtcagcctcg gcatggtgcc cggccaggtc ggcctgggcg gcgaaggcgc 4680 cggtgtcgtg acggagacag gccccgatgt cacccacctg tcggtcggcg accgcgtgat 4740 gggcgtcctc cacggctcct tcggcccgac ggccgtggcg gacacccgca tggtcgcgcc 4800 ggttccgcag ggctgggaca tgcggcaggc ggccgcgatg cccgtcgcgt atctgacggc 4860 ttggtacggg ttggtggagc tggccggtct gaaggcgggc gagcgcgtgc tgatccacgc 4920 agccacgggt ggtgtgggaa tggcggcggt gcagatcgcc cgtcacctgg gtgccgaggt 4980 gttcgccacc gccagtgcag ccaagcacgt cgtactggaa gagatgggca tcgacgccgc 5040 ccaccgcgcc tcctcccggg acctcgcctt cgaggacacc ttccggcagg ccaccgacgg 5100 gcgcggcatg gacgtcgtcc tcaacagcct gaccggcgag ttcatcgacg catctctgcg 5160 gttgctcggc gacggcggcc ggttcctgga gatgggcaag accgatgtgc gcacgccgga 5220 ggaggtggcc gcggagtacc cgggtgtcac ctacaccgtg tacgacctcg tcaccgacgc 5280 ggggccggat cgcatcgcgg tcatgatgag tgagctgggc gagaggttcg cttccggtgc 5340 ccttgaccct ctgccggtgc gttcctggcc gctggacaag gcgcgtgagg cgttccggtt 5400 catgagtcag gccaagcaca ccggcaaact cgtactcgac gtgcccgcac cgctcgaccc 5460 cgacgggacc gtcctgatca ccggaggcac gggggcgctg gggcaggtcg tggccgagca 5520 tctggtgcgg gagtggggcg tacggcacct gctgctggcc agccgccgtg gactggacgc 5580 ccccggcagc ggtgaactcg ccgacaggct gtcggacttg ggcgccgagg tgaccgtcgc 5640 ggcggccgat gtgagcgacc cggcctcggt ggtggagctg gtcggcaaga cggatccctc 5700 gcatccgttg acgggtgtcg tgcacgcggc gggcgtgctt gaggacggga tcgtgacggc 5760 tcagacgcct gaggggctgg cgcgggtgtg ggcggccaag gccgctgcgg cggcgaatct 5820 ccatgaggcg acccgggaga tgcgtctcgg tctgttcgtg gtgttctcct cggcggccgc 5880 cacgctcggc agtccgggcc aggccaacta cgcggctgcc aatgcctatt gtgacgcgct 5940 gatgcagcgc cgacgggcgg cgggccaggt cggcctgtcg gtcggctggg gtctctggga 6000 ggcaccggac gccaagccgg gtgttgccgc cgacgccaaa ccggatgttg ccgccgacgc 6060 caagacggga gttgccgccg acggcactcc ccagggcatg accggcaccc tgagcggcac 6120 cgacgtggcc cgcatggcac gcatcggcgt caaggcgatg accagcgcac acggtctcgc 6180 cctgctcgac gccgcacacc gccacggccg cccccacctc gtcgccgtcg acctcgacac 6240 ccgcgtcctg gcgcacaaac ccgccccggc cctccccgcc ctcctgcgcg ccttcgccgg 6300 agaccaggga ggccagggag gcggccgagg cggcggtcgg ggcggcggcc cggcacgacc 6360 ggcggccgcc accacccggc agaacgtcga ctgggccgcg aagctctccg tcctgacagc 6420 cgaggaacag caccgcaccc tcctcgacct ggtacggacg cacgcggcag ccgtcctcgg 6480 gcacgcgggc accgacgccg tacgcgccga cgccgccttc caggatctcg gcttcgactc 6540 cctcaccgcg gtcgaactgc gcaaccgcct ctccgcctcc accggcctgc gcctgcccgc 6600 cacgttcatc ttccggcacc cgaccccgtc ggccatcgcc gacgaactgc gcgcacagct 6660 ggcccccgcg ggggccgacc cggccgcgcc gctcttcggt gaactggaca agctggagac 6720 ggtgatcacg gggcacgcgc acgacgagag cacccggacc cgcctggcgg cacgcctgca 6780 gaacctgctg tggcgcctgg acgacacttc ggcccgctcg gaccacgcgg ccggcgcgag 6840 cgacgccgac ggcgacgccg tcgagaaccg agacctcgag tccgcgtcgg acgacgagct 6900 cttcgagctg atcgaccgag aactgccttc ttgatcagga gtggagaaga catgccgggt 6960 acgaacgaca tgccgggtac cgaggacaag ctccgccact acctgaagcg agtgaccgcg 7020 gatctcggac agacccgtca gcgcctgcgc gacgtggagg agcgccagcg ggaaccgatc 7080 gccatcgtcg cgatggcctg ccgctacccg ggcggggtgg cctcccccga gcagctgtgg 7140 gacctggtcg cctcacgcgg cgacgccatc gaggagttcc ccgccgaccg cggctgggac 7200 gtggcgggcc tctaccaccc cgacccggac caccccggca cgacctatgt acgagaggcc 7260 ggattcctgc gggacgccgc ccgcttcgac gccgacttct tcggcatcaa cccgcgcgag 7320 gcgctcgccg ccgacccgca gcaacgggtg ctcctcgaag tgtcgtggga actgttcgag 7380 cgggcgggca tcgaccccgc cacgctcaag gacaccctca ccggcgtgta cgcgggggtg 7440 tccagccagg accacatgtc cgggagccgg gtcccgccgg aggtcgaggg ctacgccacc 7500 acgggaaccc tctccagcgt catctccggc cgcatcgcct acaccttcgg cctggagggc 7560 ccggcggtga cgctcgacac ggcgtgctcg gcatcgctgg tcgcgatcca cctcgcctgc 7620 caggccctgc gccagggcga ctgcggcctg gcggtggcgg gaggcgtgac cgtactgtcc 7680 acgccgacgg cgttcgtgga gttctcacgc cagcgcggac tcgcaccgga cggccgctgc 7740 aagccgttcg ccgaggccgc cgacggcacc ggattctccg agggcgtcgg cctgatcctc 7800 ctggaacgcc tctccgacgc ccgccgcaac ggacatcaag tactcggcgt cgtacgcgga 7860 tcggccgtca accaggacgg cgcgagcaac ggcctgaccg ccccgaacga cgtcgcccag 7920 gaacgcgtga tccgccaggc cctgaccaac gcccgcgtca ccccggacgc cgtcgacgcc 7980 gtggaggcac acggcaccgg caccacgctc ggcgacccga tcgaggggaa cgcactcctc 8040 gcgacgtacg gaaaggaccg ccccgccgac cggccgctgt ggctcggctc tgtgaagtcg 8100 aacatcggcc acacgcaggc ggctgcgggc gtcgcaggcg tcatcaagat ggtgatggcg 8160 atgcgccacg gcgagctgcc cgcctccctg cacatcgacc ggcccacgcc ccacgtggac 8220 tgggagggcg ggggagtgcg gttgctcacc gatcccgtgc cgtggccacg ggccgaccgc 8280 ccccgccgcg cgggggtctc ctccttcggc atcagcggca ccaacgccca cctgatcgtg 8340 gaacaggccc ccgccccgcc cgacacggcc gacgacgccc cggaaggcgc cgcaaccccc 8400 ggcgcttccg acggcctcgt ggtgccgtgg gtggtgtcgg cccgtagtcc gcaggccctg 8460 cgtgatcagg ccctgcgtct gcgcgacttt gccggtgacg cgtcccgagc gccgctcacc 8520 gacgtgggct ggtctttgct gcggtcgcgt gcgctgttcg agcagcgggc ggtggtggcg 8580 gggcgtgaga gggctgaact gctggcgggg ctggctgcgt tggccgctgg tgaggagcac 8640 ccggctgtga cgcggtcccg tgaggaagcg gcggttgctg cgagcggtga tgtggtgtgg 8700 ctgttcagtg gtcagggcag tcagttggtc ggtatgggtg ctggtttgta tgagcggttc 8760 ccggtgtttg cggctgcgtt tgatgaggtg tgcggcttgc tggaggggga gctgggggtt 8820 ggttcgggtg ggttgcggga ggtggtgttc tggggcccgc gggagcggtt ggatcacacg 8880 gtgtgggcgc aggcggggtt gtttgcgttg caggtggggt tggcccggtt gtgggagtcg 8940 gtcggggtgc ggccggatgt ggtgctcggg cattcgatcg gtgagatcgc ggccgcgcat 9000 gtggcggggg tctttgatct ggcggatgcg tgtcgggtgg tgggggcgcg ggcgcgtttg 9060 atgggtgggt tgcctgaggg tggggcgatg tgtgcggtgc aggccacgcc cgccgagctg 9120 gccgcggatg tggatggctc gtccgtgagt gtggcggcgg tcaacacacc tgactcgacg 9180 gtgatttcag gtccgtcggg tgaggtggat cggattgctg gggtgtggcg ggagcgtggg 9240 cgtaagacga aggcgctgag cgtgagtcat gctttccatt cggcgttgat ggagccgatg 9300 ctcggggagt tcacggaagc gatacgaggg gtcaagttca ggcagccgtc gatcccgctc 9360 atgagcaatg tctccggaga gcgggccggc gaggagatca catccccgga gtactgggcg 9420 aggcatgtac gccagacagt gctcttccag cccggcgtcg cccaagtggc cgctgaggca 9480 cgcgcgttcg tcgaactcgg ccccggcccc gtactgaccg ccgccgccca gcacaccctc 9540 gaccacatca ccgagccgga aggccccgag ccggtcgtca ccgcgtccct ccaccccgac 9600 cggccggacg acgtggcctt cgcgcacgcc atggccgacc tccacgtcgc cggtatcagc 9660 gtggactggt cggcgtactt ccctgacgac cccgcccccc gcaccgtcga cctgcccacc 9720 tacgccttcc aggggcggcg cttctggctg gcggacatcg cggcgcccga ggccgtgtcc 9780 tcgacggacg gtgaggaggc cgggttctgg gccgccgtcg aaggtgcgga cttccaggcg 9840 ctctgcgaca ccctgcacct caaggacgac gagcaccgcg cggctctgga gacggtgttc 9900 cccgcgctgt ccgcgtggcg gcgcgaacga cgtgagcggt cgatcgtcga tgcctggcgg 9960 taccgggtcg actggcggcg cgtcgagctg ccgacacccg ttccgggcgc cggtaccggt 10020 cccgacgccg acacgggcct cggggcgtgg ctgatcgtgg ctcccacgca cgggtcgggt 10080 acttggccgc aagcctgtgc ccgggcgttg gaggaggcgg gcgcgccggt acgtatcgtc 10140 gaggccggcc cgcacgccga ccgggcggac atggcggacc tggtccaggc atggcgggca 10200 agctgtgcgg acgacaccac ccagctcgga ggagtgctct ccctgctggc tctcgccgag 10260 gcaccggcca ccagttccga caccacttcc cacaccagta ccagttgcgg taccggctct 10320 ctcgcgtccc acggcctcac cggcaccttg acgctgctgc acggtctgct ggatgcgggc 10380 gtcgaagcgc ctctctggtg tgccacgcgc ggcgccgtgt cgtgcggcga cgccgatccg 10440 ctcgtctccc cgtcgcaggc cccggtctgg ggactcggac gcgtggccgc cctggagcat 10500 ccggagttgt ggggcggcct ggtcgacctg cccgccgacc cggagtcgct cgacgcgagc 10560 gcgttgtatg cggttctgcg cggagacggc ggcgaggatc aggtcgcgct gcgccggggc 10620 gcggtcctcg gccgtcgcct ggtgcccgac gcaaccccgg acgtggcccc cggctcgtcc 10680 ccggacgtgt ccggaggcgc agcccatgcc gacgcgacct ccggggagtg gcagccgcat 10740 ggtgccgtcc tcgtcaccgg aggcgtcggc cacctggccg atcaggtcgt acggtggctc 10800 gccgcgtccg gcgccgaaca cgtcgtactc ctggacacgg gccccgccaa cagccgtggt 10860 cccggccgga acgacgacct cgccgcggaa gccgccgaac acggcaccga gctgacggtc 10920 ctgcggtccc tgagcgagct gacagacgta tccgtacgtc ccatacggac cgtcatccac 10980 acatcgctgc ccggcgagct cgcgccgctg gccgaggtca cccccgacgc gctcggcgcg 11040 gccgtgtccg ccgccgcgcg gctgagcgaa ctccccggca tcgggtcagt ggagaccgtg 11100 ctgttcttct cctccgtgac ggcttcgctc ggcagtaggg agcacggcgc gtacgccgcc 11160 gccaacgcct acctcgacgc cctggcgcaa cgggccggtg ccgatgctgc gagcccccgg 11220 acggtctcgg tcgggtgggg catctgggat ctgccggacg acggtgacgt ggcacgcggc 11280 gccgccgggc tgtcccggag gcagggactc ccgccgctgg aaccgcagtt ggcgctcggc 11340 gccctgcgcg cggcgctcga cgggggcaag gggcacacgc tggtcgccga catcgagtgg 11400 gagcggttcg cgccgctgtt cacgctggcc aggcccaccc ggctgctcga cgggatcccc 11460 gcggcccagc gggtcctcga cgcctcctcg gagagcgccg aggcctcgga gaacgcctcg 11520 gccctccgtc gcgaactgac ggccctgccc gtgcgggagc ggaccggggc acttctcgac 11580 ctggtccgca aacaggtggc cgccgtcctg cgctacgagc cgggccaaga cgtggcgccc 11640 gagaaggcct tcaaggacct gggcttcgac tcgctcgtgg tcgtggagct gcgcaaccgg 11700 ctgcgcgccg ccaccgggct ccggctgccc gccaccctgg tctacgacta ccccacaccc 11760 cgcaccctcg ccgcacacct gctggacagg gtgctgcccg acggcggcgc ggcagagctc 11820 cccgtggccg cccacctgga cgacctggag gcggccctca ccgacctgcc ggccgacgac 11880 ccccggcgca agggcctggt ccggcgtcta cagacgctgc tgtggaagca gcccgacgcc 11940 atgggggcgg cgggccccgc cgacgaggag gagcaagccg cgcccgagga cctgtcgacc 12000 gcgagcgccg acgacatgtt cgccctgatc gaccgggagt ggggcacgcg gtgagcgggg 12060 tggagcgggg tgtggggtcg gcgggccctg tggaacaggg tgacggactc gcgggcctgg 12120 tcgagcgggc cgaggcgctg gccgctctgc ggggcgcctt cgacggctcc ccgggcaccg 12180 gcggcagcct cgtcgtgctc agcggcgcgg tgggcaccgg caagaccgcg ctgctacggg 12240 cgtgggccga ccgcatcggc gccgatgccg acgccctggt cctgaccgcc accgcctgcc 12300 gcgccgagcg cgacctgccg cttggcgtcc tggaacagct ggtacgcagc cccggcctgc 12360 ccccggccag cgccgagcgc gcgctggcgt ggtgggacga ggaggcctcg gccacccccg 12420 gaaagacgga cgcgaacggg acgagtgcca acgggacgga cgccaacggg acgggcgcgg 12480 gacagacggg cgcggggcag gcgggcgtgg gacagacggg cgtgggcgga gagcccgtcc 12540 tggccgcctc cgccctgcga ggcctgtgcg aggtgctgcg ggacctgctc gccgagcggc 12600 ccgtcgtggt cgccgtcgac gacgcgcacc atgccgacgc ggcgtcgctc cagtgcctgc 12660 tctccgtggt gcgccggctg cggtcggcac gactccatgt gctgttcacc gagtacgccc 12720 atcagaaggc gcagaacgcc ctgctgagca gcgagttcct gcacgagccc gccctgcggc 12780 ggatccgcct ggaaccgctg tcgaaggcgg gcgtggaggc cttgctcgcc cggcacctcg 12840 acgagcggac ggcacaagac ctcacccccg tcgtccacgg catgagcgcg ggccacccgc 12900 tcctcgtacg ggcgctggcc gaggaccacc gtgcggcggg cggcgccggg gaggcgtacg 12960 gtcgtgccgt cctcagcttt ctgtaccggc acgagactcc ggtcacccaa gtcgcccgcg 13020 ccatcgctgc gttgggcgcg cacgccggac ccggtcaggt cgggcggctg ctcgatgtcg 13080 acgcggcgtc cgtcgagcgg gccgtgcggc agctgaccgt cgcggaggtg ctgcacgagg 13140 gccgcctgtg ccacccggcg ttcgcggcgg cggtcctgga cggcatgccg cccgaggaac 13200 gccgcgccct gcacggacgg gtcgccgacc tcctgcacga ggagggggcg ccggccaccg 13260 aagtggccgc ccacctcgtc gccgccgacc ggtccgacgc cccgtgggcg gtacccgtct 13320 tccaggaagc ggcccaactc gccctggacg aggaccaggt ggagaccggc gtcgactatc 13380 tgcgcgcggc ccaccagcgg tgccggggcg ccgcgcagcg tgccgcggtc gtcggtgcgc 13440 tcgccgacgc cgagtggcgg ctcgacccag caaaggtcct gcgccacctg cccgaccctg 13500 cagccatggc cccacaaacg gaccctgccg ccctggcccc acacacggac cccgcaccca 13560 cagccgcacc cacagccgcc cccaccccca cccccatccc gaccacccca cccctcccca 13620 cccacctgct ctggcacggg cgggtcgagg aaggcctgga cgccatcggc acgctcaccg 13680 ggcccggacc caacccggcg ggtgcgccgc cgatgaaccc cgcggacctg gacaccccat 13740 ggctgtgggg cgcctacctc tatcccgggc acgtcaagga gcgcctggga tccggcgccc 13800 tgtccccgca gcgctcgacc ccgccggcgg tcacgccgga gctccaaggc gcgggcacgc 13860 tgatgaacga cctgctgcac ggcggcgaac gcgacgccac cgaggccgcc gagcgcgccc 13920 tcaaccgcta ccggctcggc ccccgcacca tcgcggtcca gacggccgcg ctggccgccc 13980 tcacctaccg cgaccggccg caccgcgcgg ccgcctggtg cgacggcctc gtcgcccagg 14040 ccgacgagcg caacagcccc acctggcggg ccctgttcac cgcgtggcgt gccctgctcc 14100 acctgcggca gggcgacccg gccgcagcgg aacagcgcgc cgaaaccgcc ctcgccctgc 14160 tcggatcgaa gggctggggc gccgcgatcg gcctgccgct ggcagccgcc gtacaggcca 14220 aggcggccct cggcgatgtc gacggggcgg cggccctcct ggaacggccc gtgccccagg 14280 cggtcttcca gacccgcacc ggactgcact acctggcggc ccggggccgc tatcacctcg 14340 ccaccggctg ccactacgcc gcactgtgcg acttctacgc ctgcgggacc cgcatgagca 14400 gctggggagt ggacctgccc gcgctggagc cgtggcgcct cggcgcggcg gaagcgtacc 14460 tggccctcgg cgaaggactc ctggcacgcc aactcgtcga cggccagctg ccgttgccca 14520 cgcctgacga cggccgcacc tggggcatga cgttgcgcct gcgggcggcc acgtcccccg 14580 cgccggcccg ggccgaactc ctcgacgagg ccgtggcggt gctccgggag agcggcgaca 14640 ccttcgagct ggcgcgggcc gtcgccgacc aggctgttgc cgtacgcgaa gggggcgagg 14700 cggaacgcgc ccggctgctg gcccgcaagg cggagctgct ggcccggcgc tggggcagcg 14760 cccccgcgcc cgccaccgtc cccgaaccgc cggagcggcc aggaccggcc actccggacg 14820 ccgaactgac cagtgcggag cggagggtgg ccgagctggc cgccgaaggg ttcaccaacc 14880 gggagatctc ccggaagctg tgcgtcacgg tcagcaccgt ggaacagcac ctgacccgga 14940 tctaccggaa gctcgacgtc aggcgactgg acctccaggc agccctcggc tgaccttcag 15000 gcggccctcg gctgaccgca ggccacgcgc ctacggtcag ccttcctgag tcaggaccgt 15060 acagccgccg taggtgtagg tgtaggcgtg ggcgagatcg tcgccgcgtc cagacccacc 15120 acggccagct cctccggaag gaacggggga gcggtcagct ccgggaggcg ttcgtcggcg 15180 cgcatcgcca tcaggaaacg gttggagccc agttcggcct gcggcgcgtt gaggctcatc 15240 acgtccgtga cgatctcgga cgccttcggg gaacggatcg acgccgcggt gatggcctcg 15300 gcgaaccgca gacgctgctc ggtgtccaca ccgatgagcc gcggatccgt cgccgagaca 15360 cggcagttga cgtagtcgat gtccttggtc gcggcgagga tccacgggtc gtccacggcc 15420 gcgccgatcg ccttctgcag ggcgcgggtg ccggcgcggg cggaccccgt accctcctgc 15480 acgctccgct cgaactcgcg gtcgatcgtg gtggcgcagc gcgcggccga gctcatgccg 15540 tggccgtaga tcgggttgaa agcggtcagc gagtcgccga tgacgagcag accgtcgggc 15600 cactgttcga ggcgctccgg atagaggcgg cggttggcgc cggagcggga accgaagacg 15660 ggggtgagtg gttcggcgtc ccggagcagg tcggcgagga tcgggtggtt caggttctcg 15720 gcgaagggga tgaactcgtc ctcgtgtgtg ggcagttgcg cgccccgcgt gcaggagagc 15780 gtcgcgagcc agcggccgcc ctcgatgggg tagaccacgc cgaagcggcc gggttcgcgc 15840 acccggtcgt cggcggcgat gttcacggcg gggaagtgcg tcgtagcgcc cggcggggcc 15900 ttgaagagcc gggtggcgta ggcgacgccc gcgtccacga cgtcttcctc cagtgccggc 15960 acgccgaggg cggcgagcca ctgcttgagg cgggagccgc gcccggtggc gtcgatcacc 16020 aggtcggcct ccagctgctc ctgccgaccg ctgtcgaggt cgcggacgac gacaccggtg 16080 acccggccgc cactgccacc accacttccc gtcagctcga cggcctcggt gcgctgccgg 16140 acggtgatgt tgtcggctcc caaggcctgc tgacgtaccg tcaagtccag cagcgggcgg 16200 ctggcgacca gcgcgaactg ggtggcgggg aagcggtgct gccacccctg accggtcagc 16260 gtcaccaggt cctcggggaa gccgaggcgg cgggcgccgg ccgcgaggag gcggtcggtg 16320 gtgccgggca gcatctcctc gatgaggcgg gcgccgttgg accacaggag gtgcgcgtgg 16380 cgggcctgcg ggaccccctt gcggtgctgg ggctcctcgg gcagcgcgtc acgttccacg 16440 acggtgacgg cgtcgacgtg ccgggccagg acgtgggccg ccagggtgcc tgccatgctg 16500 gcacccagga cgacggcatg tgcgggtcgg gtggtggtca cgcgcgtatc ccttcggggt 16560 gggtggtgtc ggcgggcccg gccggatcgt ccatggtcac gtccgtgacg ccccagaacg 16620 cctggacccg gcggccgagc ccgtgctcgt cgagttcgac gatgccgacg atgcggaagg 16680 tcatcggccg cggccgctgc acggtgaccg tggtcggcgt caccacgaaa cggtcgtcca 16740 tcgacgtcat cggcgggtcc ggcacctcgt gcgtaccgca ggagacggcc agttcgagat 16800 ggcggcggag atcgtccttg cccaccatcg ggggccgccc cacggggtcc tcgaagacga 16860 tgtcgtccgt gaacaggtcg aggacgcctt cgatgtcacc ggcgttgatg cgctcggcgt 16920 agtcgacggc catctgcttg cgcgcggcct cgtcgggcat ggcacctcca ggaagggtgg 16980 gcagaccttg tgaaagtcat cgagggccgt tcggttcagc cgaggaccgt gagatcggat 17040 gtgccccagt acgacttcag atgccggatg aggccggacg cgtccatgcg gatcacgagc 17100 atcgccgtgc ggtgtatgcg ggccgtcccc ggggcgtcgg gggccttgag ccagccccgc 17160 tccgcgtaga gcgggcccac gggcaggtag tccatgacgg aggaaatctg gatcagcgcg 17220 tgcgtggcgt cctgcccggc gacgggctcg gccgcctcct cgcgcaggtg cgcggcgagc 17280 agcggttcgt agtgggcgcg cagcgcgtcg tgcccggtga cgggcgggag gccgaccggg 17340 tcctcgagga ccgcgtcggg cgcgtacaga tcgatgatcg cgtccaggtc cccggcgttg 17400 atccgccggc tgtgctccag ggcccgcttc ttgcgggcga actcgttcat cgctgcccct 17460 ccactgcctg accgtgtccg ttgccgttgc cgttgccgtt gccgttgccg tgtccgttgc 17520 cctgcccggt gggctgtccg ttgccctgtc cgctcgcgcc gtccctgccg aggtcccggt 17580 cgatgaacgc gaagatctcg tccgccgacg cgtcctggat acgtgtacga gtggccaccg 17640 cgacctcgcc ggccgtgtcc tgcggcgcgt cgagcctggc cagcgtcgcg cgcagccgcc 17700 ccgccagttc ggcccgcgcc gagccgtcct tcgaggagac cgagagcagc gagtcctcga 17760 tgcgctcgaa ctccgccagg acgtcggcga gcggatccgc cgcgcgcggg gccagctcct 17820 gccgcagctg cgcggcgagc tccgccgggt tgggatggtc gaagacgaac gtggcgggca 17880 gcttcagccc cgtcgcggcc gagagccggt tgcgcagctc caccgcggtc agggagtcga 17940 agccgagttc ccgcagcccc tgcgtcgcgt tgacgggcgt ggccgcgtcg tagccgagga 18000 cggccgcgat atgggtgcac accaggtcga gcagcgcctc ctcccgctcg gggtcggaca 18060 tcgcgccgag cgacttgagc agcgcggccg cccccgccga cacggcaccg ccgccgctct 18120 tgctcccccc gcgcaccagg tcgcgcagca gcgccggtgc ggggtggctc tgggcctgcc 18180 ggcgcatccg ggccaggtcc agacggaccg gcgcgtacag gggcagtccg ccggcccacg 18240 ccgcgtcgag gagggcgagt ccctcgtcgg cgccgagccc gaccacgccg gcgcgggcat 18300 ggcgcgcccg gtcggcgtcg gtgagccgtc ccgacatgcc gctcgccagc tcccagtagc 18360 cccacgccag ggaggtcgcc gccgcaccgc cgtcgtgccg gtgccgggcc agcgcgtcca 18420 agaaggcgtt ggcggccgtg tagctgccct ggccggggcc gccgagcagc ccggcgaccg 18480 aggagtacag gacgaacgcg gacaggtccg cgtcccgcgt cagctcgtgc aggtgccacg 18540 cggcgtccgc cttcacgcgc atcacctcct cgacctgctc ggccgtgagg ttctgcacca 18600 cggcgtcgtt cacggtgccc gcgcagtgga agacggcggt cagcgggtgg tccgagggca 18660 ccgccgcgag gagggcggcg gcttcgtccc ggtcgcccgg gtcgcacgcg gcgaaggtga 18720 ctcgcgcgcc gagcgcggag aggtcggcgg ccagttcgag tgcgcccggc gcgtcggctc 18780 cccgcctgct ggacagcaac aggtgcctgg ctccgtaccg ttccaccagg tgacgggccg 18840 tcagcgagcc gagtgctccg gtgccgccgg tgaccagcac ggtgccctcg gggtcgaagg 18900 cgggaggcag cgagaacacg gtcgtgcccg ccgagggcgg ggccgccatc gcggcgggcg 18960 cctgccggat gtcccacacg gtgatgtcga gcggcgtcag agcacggctg tcaccccgtt 19020 ccgcgggcag cccgggctcc gccgactccg tgatctcggc aagctcggtc agctcggtca 19080 gctccgcgag gatttcccgt acgcgcccgg gctcgggcgg cacgacagcc tgtccctcgt 19140 ccggacgacc gcccgcacgg tggaccacca gggccccctc gtggcggagg gtgacgtcgg 19200 ccgcgcgctc ggcgcccgaa tcatccgccg tcgacgcacc gtccacggcc tcgacccgcc 19260 accgcccggc aagagcaaga cgcagcacgg cacggccgac ggaaccggtt tcctccccga 19320 cgagcagagt ctcgccgccg cgcggcgcca cgacatccgc cagcacgtga tacgcggaca 19380 cataggcccc caaggacccg gccgcctgcg cccaactcca gcccgccgga accggcataa 19440 gcagcgcggc atcggtgacg gccaccgggc ccaccgcgtc gaacaacccc atcacccggt 19500 cgcccacggc caccgaaccg acctcgccgc cgacttccgt caccacaccg gcaccctcga 19560 cctggcccgc cgtgagcggc cccggcgccg cggcccgcac cgccacccgc acctcgtgcg 19620 gctccagcgc ccgtccggcc tcgggagcgt cgacaaggga caactgctgt ccgccgcccg 19680 cctcttggca ccgagccagc cgccacgtga gcgatccgac cggcggcacc agccgcaccg 19740 acgcgtcgtc gcgcacgagc cgtggcacgt aggcgcgccc gtcacgcagc gccaattccg 19800 gttcgccgga ggccagtacg ccggtcagcg tggccggaga agactccagt ccgtccacgt 19860 cgagcagcgt gaggcgaccg ggattctcgg cctgcgcgct gcgcaccaga ccccacagcg 19920 acgcgcccgc cagatcaccg gcggtctcac ccggccgcgc ggcgaccgcg cctcgggtga 19980 cgacgacgag acgggtcgcc gcgaacgccg ggtcgtccac ccactccttg agcagcgaca 20040 gaagggacac ggtggccagc cgcgcgtacc cggccgggtc gccgcccctg ccatcggcat 20100 ccgcaacggc cccggcacct gcgccgggcg cggcgcacac ggcgagcacg acatcgggcg 20160 cttcgccccc agccgccact ccgtcccgga gcgcaccgaa cgtgtcccac acggggccgg 20220 cggccagcgc atcggacaag gcgtcggcca gcgcaccggc cgacgtaccg cccatcgggc 20280 cactctcgac cggcgcgagg accgcggcac gcggggcgcc gccgcccgtc tcctcggccc 20340 gcgcggcgac ctccatccac acgagccgga acagcgcgtc acggtccgcc gcacgggcgc 20400 ccgcgatctg gtgggcggcc accggccgta ccgtgagcga ctccagcgtg agaaccggct 20460 ccccgcctcc gcccccgtcc acggccgtga gggccagctg gtcgggcgcg gtgcgtgcga 20520 tacgtacccg caacttctca gcgcccggcg cgtgcacccg caacccgctc caggagaacg 20580 gcagcagcac ttggtcggtg tcggcggacg acgtgaccgc gtccaggatc agcgcgtgca 20640 gcgtggcgtc gagcaacacc gggtgcacct ggtagcggtc ggccctgccg ctctccgcct 20700 cgggcagcgc cacctcggcg aaaaggtcgt ccccgagccg ccacgcgctc accagtccct 20760 gtgagccggg cccgaagtca tagccgtacg aagcgagttc cccgtacgga tcctgctcgc 20820 cgaccggtgt ggcgcccggg ggcggccacg tcccgccgaa cgaggcgtcc ccggcgtcgg 20880 gccccggggg agcgaccacg cccgcggcat gccgggtcca cacggcctcc tcgccctcac 20940 ccgtgggccg cgaatggacg gtcacgggac gccgcccgtc ctcggccacg gaaccgacca 21000 ccacctgcac gtcgaccgcg cccgcaccct cgtccccgaa ggcgagcgga gtgtgcagcg 21060 tcagctccgc caactccgcg cagccggccc gcaccgcggc ctgcagcgcg agctccacga 21120 acgccgaacc gggcagcagc accgtgtcca tgacccggtg ctcggccagc cacgcctggt 21180 cccgcggaga gatccggccg gtcagcaggt gactgccgcc gtccgcgagt tccacggcgg 21240 ctccgagcag cggatgcccc gcggacgcga gcccgagccc cgccgggtcc ccggcgagcc 21300 ccctgcgccc ctccagccag aaccgctccc gctggaaggc gtacgtcggc agatccacca 21360 cccgaggcag cggcacggcc gggaaccagc ccgtccagtc gacctccgcc cccgcgccga 21420 aggcctgggc ggccgcgcgg gtgagctgcg cggcgtcgcc gtggtcgcgg cgcagggtgg 21480 gcacgacggt ggcgggcatg tcggcccgct cgatggtctc ctccatgccg aggttgagga 21540 cggggtgggg gctggcctcg atgaacaggc ggtagccgtc ggccagcagc gcttcgatgg 21600 tgtcggcgaa gcggacgggc tggcggaggt tggtgaccca gtaatccgtg tcgagggtgg 21660 tggtgtcgtc gaggcgttcg gcggtgaccg tggagtagaa ggcgacgtcc gtggtcgtgg 21720 gccggatgtc ggccaggcgc tcggtgagga ggtcgtggag ctggtcgatc tgggggccgt 21780 gggaggcgta tccgacgtcg atgacgcggg cgcgcaggcc tcgcgcctcc gcatccgcga 21840 ccacggctgc cacatgctcc ggcggccctg aaatgaccgt agaggagggc ccgttgacgg 21900 cagcgacaca cacgccgggc cggtcgccga tgagctcagc aacctgctcc gagccggccc 21960 ccaacgacgc catgtcgccc tgccccatga gctgacggag cgcgtcactg cgtacggcca 22020 cgatccgcgc cgcatcctcc agtgacagtg cccccgccac acacgcggcg gccatctcgc 22080 cctgcgagtg cccgatgacg gcagccgggg tgatgccgta atcggcccac accgaagcca 22140 gcgagaccat caccgcccac aacacgggct gcacgacctc gacccgggac agctcactcc 22200 cgtccccgcg caacaccgca ctcagcgacc agtccacatg cgccgacagg gcccgctcac 22260 actccgcgat ccgcgccgcg aagacggggg actcgtcaag gagctgggca cccatgccca 22320 cccactgcga cccctgcccc ggaaacacca acaccggacc cgcgccggag gcgccctgta 22380 cggcgccctc gacgacgtcc ggtgacggct cgcccgccgc cagggaccgt agcccggcga 22440 ggagagtctg gcggtccttg cccacgacga cggctcggtt ctcgaacacc gaccgggtct 22500 tgaccaggga ccagcccacg tccagcggcg acgcgagccg cgggtcggcg gtggcgcggt 22560 cggccagcag gcgggcctgg gcccgcagcg cctcctcgcc gcgcgccgac accacccagg 22620 gcaccactcc ggccggcgcc gcggcgtcct ccgccggagc ggtcacgggc tccggcgcgt 22680 ccggggcctg ttccaggatg aggtgcgcgt tggtgccgga gatgccgaag gcggacaccc 22740 cggcgcggcg cgggcgttcg ccgcgcggcc aggagaccgg ttcggacagc aggcggacgc 22800 cactgccgtc ccagtccacg tgcggcgtgg gcgcgtcgat gtgcagggag gcgggcagct 22860 gttcgttgcg cagcgccatg accatcttga tcacaccggc gacaccggcc gacgcctgcg 22920 cgtgcccgat gttcgacttg atcgagccga gccacagcgg ccggtccgcg ggccgctcct 22980 tgccgtaggt ggcgacgagc gcgctggctt cgatggggtc gcccagcatg gtgccggtgc 23040 cgtgcgcctc caccgcgtcg acgtcctcgg cggagagccg cgcgttggcg agtgcctgcc 23100 ggatcacccg ctgctgcgcc tgcccgttgg gtgccgtgag cccgttgctc gtgccgtcct 23160 ggttgatggc cgaaccccgg atcaccgcca ggacgttgtg gccgttgcgc cgggcctccg 23220 agagccgttc gagtacgacc aggccgactc cctcggccca gccggtgccg tcggcggcgg 23280 ccgcgaacgg cttgcaccgg ccgtccttgg cgagcccgcg ctgcagcgag aactcgacga 23340 acgagcccgg cgtggccatc accgtcgcgc cgcccgcgag agcgagcgag cactcgccct 23400 ggcgcagcgc gtgcgccgcc tggtggatcg ccaccaggga cgaagagcag ccggtgtcga 23460 tcgtcatggc ggggccttct aggccgagta cgtacgacac cctgccggag gcgacacagc 23520 cgaggttgcc ggtgccgatg tagccctcga cctcggtggg ctgttcaccg acgagcgcga 23580 ggtagtcgaa gatggtcagg cccgtgaaca ccccggcgtc gctgcccttg agggtctccc 23640 ggtcgaggcc cgcgcgttcg atcgcctccc acgcggtctc caggagcagc cgctgctgcg 23700 ggtccatcgc gacggcctcg cgggggctga tgccgaagaa tccggcgtcg aagtcgcccg 23760 cgtcgtagag gaacccgcct tcgcgcacat agctggtgcc gcggctctcc gggtccgggt 23820 cgtacagcgt ctccaggtcc cagccccggt cgtcggggaa ggcccccatg gcgtccttgc 23880 cggccgcgac cagatcccac agctcctcgg cggagcggac gtcgcccgga tagcggcagg 23940 ccatgccgac gatcgcgatc ggctcgtcgt cggcggcgcc cctggaggcc ccggccgccc 24000 gcaccgggtc ggcggaggcc gccgcgtcac cggacagctc ggcccgcagg acgtcggtga 24060 gcgcgtcggg ggtggggtgg tcgaagacga ccgtggtcgg cagtgtcagg ccggtgctct 24120 tgttcagcct gttgcgcagc tccaccgcgg tcagcgagtc gaagcccagc tcctggaacg 24180 gcttggtggc gggcaccgcg tcgacgtccg agtgccccag cgtggccgcc gcctgggagc 24240 gcacgtgctg cagcagcaac tgccgctgct gcgccggctt cgcctccgtc agctcctgct 24300 ggagcgacga tgcctccgtg gcgtcttcct gctgtgccgc gggtgcgctg gcccgccggt 24360 tctcgggcag atcggcgagg agcgggctgg gccgctgcgc ggtgaacgtc gacgtgaact 24420 gcgcccagtc gaagttcgcc acggtcagcg tcgtctcacc cgcgtccagg gcctgctgca 24480 gcgccttgac gcacagctcc gggctgagcg ggtgcaggcc gaagcggctg aagaacgtca 24540 acgcggcctg gtccgccgcc atgcccgcct cggcccaggg cccccaggcg atggaggtgg 24600 cgggcaggcc ctcggcgcgg cggtgctcgg cgagggcgtc gaggaagtgg ttggccgcac 24660 cataggcgcc ctgctggcca ctgccccaca cgcctgcgcc cgacgagaac atcacgaacg 24720 ccgagagcgg caactcccgg gtcagttcat gcagatggtg agcggcgagc gccttcggac 24780 gcagcacctc gtccagctcg gcacccgaca cgtcgccgag accgatgtag ttcggcacgc 24840 cggccgcgtg gatgacggcg gtcagcgggt gctcggcggg gacatcgtcg atgaggcgtc 24900 gcacctgctc gcggtcgccg acgtcgcagg cggtgacggt gacggcggcc cccaactccg 24960 tcagttccgc ggcgagttcc tgtgctcccg gggcgtcggg gccgcggcgg ctggtcagga 25020 ggaggtgcgg ggcgcccgca cgggcgagcc accgcgcgag gacggcgccg atgccgccgg 25080 tcccgccggt gatgagagtg gtgccgtcgg gccgccaacc aagcccgctg ccgaccgtgt 25140 tggcgggcgc gtgtgcaagg cgacgggcat ggacgccgga cggccggatg gagatctggt 25200 cctcgtcctg cggaaccagc gcggcggcca gccgggccag cgtctgatgg tcgatacgag 25260 cgggcagatc gaccagcccg ccccacagcc gcggatactc cagcgcagcg acgcgcccca 25320 gcccccacac ctgagcctgc accgggtggg tgagggcgtc gccggcgctc gtggaaacag 25380 ccccctgcgt gagagtgcgt acggcgatgt cggcgccgtt gtccgcgagg gcctggacga 25440 gagcggtcgt cgcggcgagt ccggcgggca cggccgagtg ctcgggatgc ggctcctcgt 25500 ccagggccag cagattgacg actccggcaa acgcggcccc gtccatcagg acacgcagct 25560 cctgcgccaa ctccgtacgc tccatggcac gtgcgtcgac cacgtggcgt cgcacctcgc 25620 caccatgggc ggtcagcgtc tgcgcggtcg cgaggacggc cgggtggtcg gcgtgcgcgg 25680 cgggcacgag cagcagccag gccccgctga gctccggcgc cggcacgtcg ggcagatgct 25740 tccaagtgac ctgataacgc caggagtcga cggtggactg ctcgcggtgc cgacgccgcc 25800 aggccgagag gacgggcagc gcggactcca gcgctccgac gctctccgcc tgcccctcga 25860 tctccagact gccggcgagg gcgtcgatgt ccaggtcctc gatcgcctgc cacacccggg 25920 cctcgaccgg atcgtgccca ccacccacgg ctgcgaccgc cgcgggcggc tccacccagt 25980 agtgcttgtg ctggaaggcg taggtgggga ggtcgacggt acggggggtg gggtcggccg 26040 ggaaccagcg ccgccagtcg acgggggcgc cggcggtgaa ggcgtgggcg gccgcgcggg 26100 tgagctgggt ggtgtcaccg tggtcgcgac gcagggtggg gatggtgacg gccgtccccg 26160 cagcaccggc ctgctgctcg atggtctcct ggatgccgag gttgaggacg gggtgggggc 26220 tggcctcgat gaacaggcgg tagccgtcgg ccagcagcgc ttcgatggtg tcggcgaagc 26280 ggacgggctg gcggaggttg gtgacccagt aggcggtgtc tagggcggtg gtgtcgtcga 26340 ggcgctctgc ggtgaccgtc gagtagaacg ccacgtcggt ggtggtcggc tggatgtcgg 26400 cgagccggtc ggtgaggagg tcgtggagct ggtcgatctg gggaccgtgg gaggcgtacc 26460 tgacgtcgat gacgcgggcc ctgagtccct gcgcctccgc atcggcgacg acggctgcca 26520 catgctccgg cgggcccgaa atcacggtcg acgacggtcc gttgacggcc gcgacgacta 26580 cgcccggccg gtcgccgatc agctctgcgg cctgctcggc accggtgctg agcgaggcca 26640 tgtcgccgtg cccttgcagc tgacgaagcg cgtcgctgcg tacggctacg atccgtgccg 26700 catcctccag tgacagtgcc cccgccacac acgcggcagc catctcgccc tgcgagtgcc 26760 cgatgacggc agccggggtg atgccgtaat cggcccacac cgcagccagc gagaccatca 26820 ccgcccacag cacgggctgc acgacctcga cccgggacag ctcgctcccg tccccgcgca 26880 agacatcact cagcgaccag tccacatgcg ccgacagcgc ctgctcacac tccgcgatcc 26940 gcgccgcgaa gacgggcgac tcgtcaagga gctgggcgcc catgcccacc cactgcgacc 27000 cctgccccgg aaacaccaac accggcccag gacccacatc accggccacc ccggccacca 27060 catccgccga cgcctcaccc gcggccaatg cctccaggct ggcaccagcc tgagccaagt 27120 cccgccccac gaccacggcc cgctgatcga acaacgcgcg tgtcgtggcc agcgaccagc 27180 ccacctcgga gaccgacgca tccgccagcc cggccgcgaa ctcgcccagc cgccgcgcct 27240 gttcacgcaa cgcgtccggc gtccgcccgg acaccaccca cggcacgacc ccacccggct 27300 cagccgccac ggggcccggc gcgtcctctt ccggcggcgc ctcctccaga atcaggtgcg 27360 cgttcgtccc ggagatcccg aacgccgaga tgcctgcccg ccgcgtgcgc tccgccggcc 27420 agtccacggg ctcggagagc agtcgtacgc tgccctgttc ccactggacg tgcggtgacg 27480 gggcgtcgat gtgcagggag gtcgggagga gaccgttgcg catcgccatg accatcttga 27540 tgacgcccgc gacaccggcg gcggcctgcg tgtggccgat gttggatttc accgagccga 27600 gccagagcgg acggtcctcc gggcgcccct ggccgtacgt ggcgatcagg gcctgcgcct 27660 cgatggggtc gccgagcgtg gtgccggtgc cgtgcgcctc tacggcgtcg atgtcctcgg 27720 cggagaggcg ggcgttggcg agggcggcgc ggatgacgcg ttcctgggag gggccgttgg 27780 gggcggcgag cccgttgctc gtaccgtcct ggttggtggc cgaaccccgt atcaccgcaa 27840 ggaccttgtg gccgcggcgc cgcgcttcgg agagcagctc cagcgccacc accccggcgc 27900 cctcgcccca gccggtgccg tcggcggcgg ccgcgaacgg cttgcaccgc ccgtcgggcg 27960 cgagcccccg ctgccgggag aactcggtga acgaacccgg cgtcgccatc accgtcgaac 28020 cgcccgccag cgcgagcgag cactcgccct gccgcagcgc ctgacttgcc agatggatcg 28080 ccaccaggga cgacgagcac gccgtgtcga cggtgaccgc gggaccttcg agccccaccg 28140 tgtaggagat ccggcccgac accacactgc cgaggttgcc ggtgccgatg tacccctcga 28200 cgtcgctggc cgtctggctg atcagcgtca ggtagtcgtg ggcgctcact ccggtgaaga 28260 cgccggtgtc gctgcccttc agcgcgtgcg ggttcatgcc cgcgtgctcg atcgcctccc 28320 acgcggtctc caggagcagc cgctgctgcg gatccatcgc cgtggcctcg cgcgggctga 28380 tgccgaagaa ctcggcgtcg aaatggccgg cgtcgtacag gaaggcgccg tcccgcacat 28440 agctggtggc cggatgctcc ggatccgggt gatacagcga ctccaggtcc cagccccggt 28500 cgtcggggaa ccccgcgacc gcgtcacccc cgtcgcgcac gagttcccag aggtcctccg 28560 ccgaccgggc gccgcccggg tagcggcagg ccatgccgac gatggcgacc ggctcggtcg 28620 attccttgtc gtggagccgt tgccgggcct ggcgcagctc cgcggtgacc cacttgaggt 28680 gatcgagaag cttctcctcg ttcgacatct gacccaggct ccttggcgct acgtggtgat 28740 cggggcgtat gaggttgggg gagggcaagg gggccggtgt ggccggggct catcgcgctc 28800 aggactgatc gctgctcagg acttcccgaa ctcactggag atgaggtcga agatgtcgtc 28860 cgcgctcgcc gcctccagat cggcatgggc cgaatcagtg ccttccggcc cgtcctgcgc 28920 cggactccac ttcgacacaa ggacctgcag ccggcccacg atgcggcgcc gggccgcctc 28980 gtccacctcg gccgctccga acgccgtgtc ccacttgtcg agcgccgcga gcacgtcgcc 29040 ctcacctgcg acctcggcgc cgtcgccgag ctgtccgcgc aagtgcgtgg cgagggcctc 29100 gggcgtggga tggtcgaaga tcacggtggc ggggagcgag agtccggtcg tggtgttgag 29160 ctggttgcgc agctggaccg cggtgagcga gtcgaagccc agctcctgga acggcttcgc 29220 ggcgggaatg tcctccaccg tgcggccgag cgtcgcggcc gcgtatgtcc ggacctgctg 29280 gaccaggaag ccgagccgct gtgatgcggg cgtcttcgcc agctcctcgc ggaacgcgct 29340 cgtctcggcg gcggtccccg tctgctcggc ctcccgctgg ttctccggaa ggtcgtcgag 29400 gaacggactg ggccgctgcg cggtgaacgt cggcgtgaac ttcgcccagt cgaagttcgc 29460 cacggtcagc gtggcgtcgc ccgcgtcgac cgcctggtgc agcgccttga cgcacagatc 29520 cggagcgatc gggagcagac cgaagcgctt gaagtacgtc agtgactccg ggtcggcgga 29580 catgcccgcc tcggcccagg gcccccaggc gatggaggtg gcgggcaggc cctgggcgcg 29640 gcggtgctcg gcgagggcgt cgaggaagtg gttggccgca ccataggcgc cctgctggcc 29700 actgccccac acgccggcgc ccgacgagaa catcacgaac gccgagaggt ccaggtcgcg 29760 cgtcaactcg tgcaggttcc aggccgcgtc ggacttcgac cccagcacct cgccgaggcg 29820 cgcggtcgtc agatcaccga tcgcggtcag atcggtcatg cccgccgcgt ggatgacggc 29880 tgtgagggga tgctcggccg gcatgtcgtc gatgaggccg ctcagttggc ggggatcgct 29940 gacgtcgcag gcggtgatgg tgacggcggt gccgagcccg tcgagctcgg cggcgagttc 30000 4 13600 DNA Streptomyces cinnamonensis Nucleotides 90001 - 103600 of the monensin biosynthetic gene cluster 4 ccgggcgccg ggcgcgtcgg gcccgcgacg gctggtgagg tgaagacggg gggcgccctg 60 ccgggccagc caacgggcga ggacggcacc gatgccgccg gtcccgccgg tgatcagggt 120 ggtgccccga ggccgccagg tggcctcgct gtgcacggga ttctgaatgc ttccgacggc 180 gtgcgtgagg cgccggtggt ggattccggt ggggcggacg gcggtctggt cctcgtcgtc 240 ctgggggagg agagcggcgg cgaggcgggg gagggtgtgg cggtcgatac gagcggggag 300 gtcgacgagt ccggcccaga ggcgcgggtg ttcgagggct gcgacgcggc cgagccccca 360 gacgtgagcc tggagggggt gggtgagtgg gtcggtggcg cccgtggaca cggcaccctg 420 cgtgacggtg tgcaggggtg cggtcgtgcc gttgtcgccg agggcctgga ggagagcggt 480 cgtcgcggcg agccccgcgg gcacggcggg gtgctcgggg tgcggctcct cgtccagcgc 540 cagcagattg acgattccgg caagaccggc cgtgtccacc gcggccagct cctgacgtcc 600 cgcccggccg gtctcgaccg gatgcagccg gacggcggcc gccccgtgct cgctcaacgc 660 ctcggcggtg gctcgtacgg cggggtgctc cgccttgtcg gcagggacga acagcagcca 720 gtcgccgccg agttccggtg cgggcccgtc ggaccgctgt ttccacgtga cgcggtaccg 780 ccaggagtcg atggtcgcct ggtcctggtg ccgacgccgc cagcccttga gcaccggcaa 840 cgcgggctcc agcgcccgga ccgcctcctc gctgccctcc tccgacccca gcgtctcggc 900 cagcagaccg agatcgagct cctcgacggc gtgccacagc tgggcctcgg ccgcactctg 960 ctcaccgctg acggcgcccg aggcggacgc ggaacgttcg agccagtagt gctggtgttg 1020 gaaggcgtag gtggggaggt cgacggtgcg gggggtgggg tcggccggga accagcgccg 1080 ccagtcgacg ggggcgccgg cggtgaaggc gtgggcggcg gcacgggtga gctgggtggt 1140 gtcgccgtgg tcgcggcgga gggtggggac gacggtggcg gggatgtccg cctgctcgat 1200 ggtctcctcc atgcccaggc ccagcacggg gtgggcgctg gcctcgatga acaggcggta 1260 gccgtccgcg agaagggctt cgatggtgtc ggcgaaccgg accggctggc ggaggttggt 1320 cacccagtaa tccgtatcca gggctgtggt gtccgtcaga cgctcggcgg tgaccgtcga 1380 atagaaggcc acgtccgtgt tcgcgggccg gatgtcagcc aggcgttcgg tcagcagatc 1440 gtggagctgg tcgatctggg ggccatgcga ggcgtacccg acgtcgatga cacgggcgcg 1500 cagaccacgt gcctccgcat cggcgaccac ggcagccaca tgctccggcg gccctgaaat 1560 caccgtagac gacggcccat tgaccgccgc gacgaccacg cccggccggt caccgatcag 1620 ctcagcggcc tgctcggcac cggtgctcag cgaggccatg tcaccgtgcc cttgcagccg 1680 acgaagcgcg tcactgcgta cggctacgat gcgcgccgca tcctccagcg acagcgcccc 1740 cgcgacgcac gcggcagcca tctcaccctg cgagtgcccg atcacagcag ccggagtgac 1800 cccgtaatca gcccacaccg cagccagcga gaccatcacc gcccacaaca ccggctgcac 1860 gacctcgacc cgggacagct cactcccatc cccgcgcaac accgcactca gcgaccagtc 1920 cacatacgcc gacagcgccc gctcacactc cgcaatccgc gccgcgaaga cgggggactc 1980 gtccagcagc tgggcaccca tgcccaccca ctgcgacccc tgccccggaa acaccaacac 2040 cggcccagga cccacatcac cagcaacccc ggccaccaca cccgccgaag cctcacccgc 2100 agccaacgcc cccaggccag ccgtcaacgc atcgcggtca cgccccacca ccacagcccg 2160 gtgctcgaac accgaccggg tcgtggtcaa cgaccagccc acatcagccg ccgacgcatc 2220 cgccggcccg gccgcgaact cgcccagccg ccgcgcctgt gcacgcagcg cgtccggcgt 2280 ccgcccggac accacccacg gaacgacccc acccggctcc tcggccacgg agcccggcac 2340 gtcctcctcc tccggtggtg cctcctccag gatcagatgc gcgttcgtcc ccgagaagcc 2400 gaacgaggac acccccgccc ggcgcgggcg ctcgccccgg ggccacttca ccgggtcggt 2460 gagcaggcgc agcccgctgc cgtcccactc cacgtggggc gagggggcgt cgacgtgcag 2520 gatggcgggc agcaggtcgt gccgcagggc caggaccatc ttgatgacac cggccacacc 2580 ggcggcgatc tgcgtgtggc cgatgttgga cttcaccgct cccacccaca gcggccggtc 2640 ctccggccgt tcccggccgt aggcggagat gagagccccg gcctcgatgg ggtcgccgag 2700 cgtggtgccg gtgccgtgcg cctccacggc gtcgatgtcc tcgggggcga ggcgggcgtt 2760 ggcgagggcg gcgcggatga cgcgttcctg ggcggggccg ttgggggcgg tcaggccatt 2820 gctcgcgccg tcctggttga tcgccgaacc ccggatcacc gcgaggacct tgtggccctt 2880 cctgcgggcg tcggagagac gctcaaggag aaccaccccc gtaccctccg ccatgcccat 2940 gccgtcgctg ctcgccgaga acggcttgca ccgtccgtcg ggggccaggc cgcgcagttc 3000 gctgaagccg atcagcgggg cgggcgacga catcacgtac gtgccgcccg ccagcgccag 3060 cgagcactcc tgtgtgcgca gggcctgggt ggcgaggtga agggagacca gcgacgagga 3120 gcacgccgtg tcgaccgtca ccgcggggcc ttcgaggccc agggtgtagg cgacgcggcc 3180 ggaggtgacg ctgccggagt tgccgatggt gaagtatccg gcggtgccct cggggacctc 3240 ggacgcgccg agggcgtagt cgagtccgtc acagccgatg aaggtgctgg tgtcgctgga 3300 gcggaggctg agggggtcga tgccggcccg ttcgatcgcc tcccacgccg tctccagggc 3360 gagccgctgc tgcggcgcca tggccgcggc ctcggtgggt ccgatgccga agaaggtggg 3420 gtcgaagtca ccggcgtcgt agacgaagcc gccttcccgg acgtaactgg tgccggtgct 3480 ctcggggtcc gggtcgtaga gggaatcgag gtcccagttg cggttgccgg gcaggggcgc 3540 gacggcgtcg ccgccggtgg agaccagctc ccagaactct tcgggagacc ggactccgcc 3600 gggcagccgg caggccatgc cgatgaccgc gaccggttcg tggcccgccg actcgacgtc 3660 ctgcagccgg cgttccgtct gacgcaggtc cgcggtgaca cgcttgaggt attccagaag 3720 tttctcttcg gtgtgcgcca tcccggtgac aaccgcccct ctccgcgaga acagaccgca 3780 gactcgtcga cggcgctaaa gccctcctaa tactcggctg tgtaccgctc gctgccacgg 3840 gtgtccgcac tggtcggagg ctccggccca gggaacaggg gctttcttag gggcgcttaa 3900 gcggtgcctg ccagggtgtg ccggtgtcag gccgtcacgc cctgatcagc ggcgtcgccc 3960 gtgccgtgcc cgtgcggtcg gtgggcctga ccgtcggtcc ggacaacgcg aagcgaggca 4020 tcgtgcccat cacggatagc aagccggccg ccacattccc cgacctggtc gacccgtcgt 4080 tctgggcgcg gccgcacgcg gaacgcgtgg cgctgttcga ggagatgcgc gggctgccgc 4140 ggccggcgtt catccggcag aacatgcccg gcgtgccctg gacgttcggc taccacgcgc 4200 tggtcaagta cgcggacatc gtggaggtga gccgccgccc gcaggacttc tcctcgaacg 4260 gcgcgaccac catcatcggt ctgccgcccg agctggacga gtactacggc tcgatgatca 4320 acatggacaa cccggaacac tcgcggctgc ggcgcatcgt ctcgcgttcc ttcggccgca 4380 acatgatccc cgagttcgag gccgtggcga cccgcaccgc ccgccgcatc atcgacgagc 4440 tcatcgcgcg gggacccggc gacttcatca ggcccgtcgc cgcggagatg cccatcgccg 4500 tgctcagcga catgatgggc atcccggcgg aggaccacga cttcctcttc gaccggtcca 4560 acacgatcgt cggccccctc gacccggact acgtgccgga ccgggcggac tccgaacgcg 4620 cggtgatcga ggcgtcacgc gaactcggcg actacatcgc tggccttcgt gcggaacggc 4680 tcgccgcccc cggcaacgac ctcatcacca agctcgtgca agtccaggcg gacggcgagc 4740 agttgacgcg gcaggaactc gtctccttct tcatcctgct cgtcatcgcc gggatggaga 4800 ccacccgcaa cgccatctcg cacgcgctgg tactgctgac cgagcatccc gagcagaagc 4860 agctgctgct ctcggacttc gacacgcacg cgccgaacgc ggtcgaggag atcctcaggg 4920 tctccacgcc catcaactgg atgcggcgcg tcgccacccg cgactgcgac atgaacggcc 4980 acaggttccg caggggcgac cggatcttcc tgttctactg gtcgggcaac cgggacgaat 5040 ccgtcttccc tgacccgtac cggttcgaca tcacgcgcgg gacgaacgcg cacgtcacgt 5100 tcggcgcggt gggcccgcac gtctgcctcg gggcccacct cgcccgtatg gagatcaccg 5160 tcctgtaccg ggagctgctc gcggcgctgc cccagatcca tgccgtgggg cagccccgca 5220 ggctggactc cagcttcatc gaagggatca agcacctgca ctgcgccttc tgagcacata 5280 cgcttccctc tgcgcatgtg cgctcacgac gctccgatca gcgactgcca acgactgtca 5340 gcgaccggac agggccaagg gcggtgggga catcaggtgc atgtcacccg cgagtatggc 5400 ccgctgcagc tcctggagcg ggcgcccggg ttcgagcccc agctcgtcgt tgagcgtctt 5460 gcgcaccgac tggtacacct tcagcgcgtc cgcctgccgc tcggagcggt agagcgccag 5520 catcagctgg cggtagaacg cctcgcacat cgggttctcc gcggtgaggg cgtacagcat 5580 gcccacggcc tcgcggtgcc ggccgagctg gagctggcac tcgacgagca tctcctgaca 5640 ctccaggcgg atctcggtca gccaggtcga gaagccgtcg atgatcgggc cgttggtgcc 5700 gggaccgttc ccgccctgcc cgaggatcgg gccgcgccac agcgcgagcg cctgcccgaa 5760 acaggaggcc gcctcgtcga accgcttctc cctgagcaac gaccgcccca cgtccaccag 5820 ttcggggaag atctgggcat cgatctggtc gtcgtcccgc ttgtgcagga cgtaccccgg 5880 cgcacgggtc tcgacggggt tgcccgccga accgggcacc ttgaggaact tgcggagctg 5940 ggagatgtac acatgcagtc ccgccgtggc gcgccgcggc aggtcctcgc cccagatctc 6000 ccgcatcagc tgctccaggg agaccacccg gtcggcgcgg atgaggagca cggtgaggac 6060 gatctccacc ttctgggcgt tgatggtggc gtagtcgttt ccgtccttga tgcggagcgg 6120 gcccagcatt tcgtatctca ccgagcgttc ccccttgctg tcgcacgctg ctgcgcactg 6180 tcggccaggg ccttggagat gacttccgtg acgccctgct ggtgcgtgtt cagatagaag 6240 tggcccccgg cgaagacctt gaggtcgaag gggccttccg tgtgctgctg ccaggcctcg 6300 acctcgtcca gcggcgcctg cgggtcccgg tcgcccacca gggcggtgat ggggcaggac 6360 agcggcggcg acgggttcca ccggtacagc tcgaccgccc ggtagtcgtt gcggacgacc 6420 gggatgatct ccgcgagcag ttcctcgtcg tccaggaacc gcgggtcagt gccaccggcc 6480 cggcgcagct cggcggccaa ctcggtgtcg tcgaggaggt gtacggtgcc gcgccggaag 6540 cgggacggcg cgcggcgtcc cgagacgaac agccggcagg gctgcttccc cgtgcgctcg 6600 cggagccgct gggcgacttc gtaggcgagg acggcgccca tgctgtggcc gaagaacgcc 6660 aacgggcggt cgtcgaacgg gccgagcgca tcggtgatga ggtcggcgag ttccccgatg 6720 tcgtccagga gccgctctct gcggcggtcc tgtcgcccgg ggtactgcac cgcgaggacc 6780 tcgctgtcgg tcgggagagt gggggattgc gcaagggggt ggtagtagga ggccgagccg 6840 cccgcgtggg ggaagcagac caggcgaacg acggcttccg gtcggggccg gaagcgacgt 6900 atccaagggt ccgacatatc gggtgggggg aaggcagaca agatctttcc cttcgccagg 6960 aacgctgaca acggtgtgtc gccacatcac atagccgctc ctgatcatgc gcagctcaaa 7020 gtttaaacgg caacgtcgct aacgggggag cagggcggaa tcagacattc cccatccttt 7080 attccgcgat tcttacgtga tcgaatcccg gcggccaaga tggagtaaat ttcaatatga 7140 atgcttaacg ccgcacagct tgtacggcgg gccgcccggg cggtgactgg cgtccctgcc 7200 agccgtgatg gcctgacgag gcctccggga tccatccccc gcccgctgtc gccgagttct 7260 ttgcgggatt attacgttgc attggtttgc ttcgtggccc gggccgttgg cctgcgctat 7320 ttggcagcct tccgtcatgg gtggtaaaag atcgcctttc ccctctgggg tgccggtcga 7380 gctggcctcg accgcgattg tggcttgttg ttttcttgtg gcgccgcgtg tgaaacagcg 7440 gcagttggcc actcgctctg acaggctccg gggacggggt tgtcaccttt tggggtgact 7500 ggcctcgttc aaggcgtcct ggcccgtggt gcatccgcga tcgtcgtgcc atgggtgaag 7560 tgggaaggag cacagaacga tgagcgagag catggcgtgg ctgacgcggg acgtccgcaa 7620 ggcccgcaag gagggcagtg cggggaccgc gcggcgccga gccgaccggc tggcggacct 7680 ggtcgcccac gcccgctcgg cgtcgccgta ctaccgggag ctctaccacg gcctgcccga 7740 gcggatcgag gacccgacgc tgctgccggt gacggacaag aagcagctga tggaccactt 7800 cgacgactgg ccgacggacc gcgacatcac cttcgagaag gtccgcgcgt tcaccgacga 7860 ccccgagctg atcgggcggc gcttcctcgg ccgctatctg gtggccacca cgtcgggcac 7920 cagcggcagg cgcggcctgt tcgtgctcga cgaccggtac atgaacgtgt cctccgccgt 7980 ctcctcccgg gtgctcgcct cctggctcgg ccccctcggc atcgcccggg ccgtcgtcca 8040 cggcggccgc ttcgcccaac tcgtcgccac cgagggacat tacgtcggct tcgccggata 8100 ctcccgcctg cgccaggacg gcggagcgcg cagcaagctc gtccgcgcct tctctgtgca 8160 cgagccgatg tcacgtctgg tcgccgaact caacgagtac cggcccgcgt tcgtcatcgg 8220 ctacgccagt acgatcatgc tgctcaccgc cgaacaggaa gcgggccggc tgcacatcga 8280 cccggtgctg gtcgagcccg cgggcgagac gatgaccgag agcgacaccg accgcatcgc 8340 tgcggcgttc ggcgccaagg tgcgcacgat gtacagcgcg accgagtgca cctacctcag 8400 ccacggctgc gccgagggct ggtaccacgt caacgacgac tgggccgtgc tcgaaccggt 8460 cgacgccgac caccggccca ccccgccggg ggagttctcg cacaccaccc tgatcagcaa 8520 cctcgccaac cgcgtccagc cgttcctccg ctacgacctg ggcgacagcg tcatgctccg 8580 ccccgacccc tgcccctgcg gcaccccctc gcccgcgatc cgggtccagg gcaggtcggg 8640 cgacatcctc accttcccct cgggccgggg cgacgacgtc agcctcgccc cgctcgcctt 8700 cagcagcctc ttcgaccgca tgcccggagt cgagctcttc cagatcgagc agaccgcgcc 8760 gtcgaccctg cgcgtccgcg tggtccaggc gcccggcgcc gacgcggacc acgtgtggca 8820 gcgggcccac gacgggctga cccacctcct cgccgacaac aagctcgaca acgtaaccgt 8880 cgaacggggc gaggagccgc cgcggcaggc atccggcggc aagtaccgga cgatcatccc 8940 gctcgccgcc tgaacgctcg ccgactagcc gcgcgccgcc tgagctgctc tcaccgcgcg 9000 tacgggcgca gcggaggctc ctcgtcgacc cacggctggc tgtggatcag cagctcgatc 9060 gggaagttca gcaggccggg cagggcgtcg acggcctcct ggctgttgag cggcatgacc 9120 ggcttggcgc agtgcgcgcg gtcgatgcgg ctcgtgtcgg cgggaccggg gtgctcgatc 9180 gcatcggcga ccaggtcgta gctgacctgg tcgacgacca tggcgatgtg ggtcggccac 9240 ggccgacccg gacagatgtc ctggacgccg atgcggtggg cgcccggcag cgacggcgcc 9300 tccccgtcgg ccaccacgga ctcgtcggcg tatgaataga tcgtggtgta cgacggtcct 9360 gcgggcatgg gcgtgccgtc ggcgcccaga gccttcgacc agttcgagtc gcgggcgaac 9420 tgcaggaccg acgccgggca gcccgccacc tcggcgatcg ggcggcaggg cgaggccagc 9480 cgggtcccct ggaacgggga gcccagggtc accatgtcgt cgaccttccc cggcaggtcc 9540 ggccagaagc gcagggccca cgccgtgagg aggccgccct ggctgtgccc gacgagatcg 9600 accttccggc cggtggcctc ctggatcgcg cgggtcgcgt acaccacgta ctcgacggac 9660 tcctgcatgt cacggagccc gcgaccggga gaatccaccc aacaggactg gtagcccttc 9720 ttcttcaact cggccatgta gttccaggcg tagttctcct cgcccttgag gccggtcccg 9780 ggcacgaaga ggacggtcgg cttgtcaccg gcgtcacgca ggtcccccag ctccgtcccg 9840 cagtgcagcg ccttggcgag ctcggccgcc ggtatctcca acgggggaga ggaaacatcc 9900 gccgccgaag cggcggaggc cggaagcacg gtggcggcca gcacggccgc cacgagtccg 9960 ccgagccatg aggacaagcg cacggtgacc tccacaggaa ccttcacgag tgagcggaaa 10020 ctccctccgg agggagcacc tcatcgtgcg gcggcgccac agtagccgtc aactgcccca 10080 cggggctgag tagttgacag ttggccgggc tcggccggcg aagcgcccgg gccccgccgc 10140 cccgcgccgt gcgcgagggg tccgtgacct gggtggacgg tccggttgga catcccgggg 10200 gagcctctgg catggtcgcc cgtccgtccc cctcaagaac cgaagggagc gtcacgatca 10260 cgatgatcga agtcagcacg cgcagcatga aggaagcggc tgccgccgag cagctccgcg 10320 cggagaccac gacactggac attccaaagg gtttcgacct gtggacggcc gacgagatcg 10380 cggagtggct cgacggcgtc gaggacgacc cggcagtctc cgacgccgac ttctacgcgg 10440 cccagcagcg gtgcgacggg tcctcggcac cgagggcacc tgacccgccg gcggccctgc 10500 gcggccctac gtgtgcagcg ccccgtcctc ctccacatgc ccctccggct ccagctggat 10560 cgtcgagtgg gccacgtcga agtggccccc gacacaccgc tgaaggcgcc ccaggagctc 10620 cccgtacccg ctcgcgagag cctcctccgt gaccaccacg tgcgcggtga gcaccggcat 10680 ccccgaggtg accgtccagc cgtgcagatc gtgcacggcg accacgcccc gctcctccag 10740 caggtgccgg cgcacctcgc cgaggtcgac gtcctgcggg gtcgcctcca gcaggacgtg 10800 caaggagtcc cgcagcaggc cgtacgcgcg cggcacgatc agcaggccga tgacgatcga 10860 cgcgatcggg tcggcggcct gccaccccgt gagcaggatg accaggccgc ccacgatcac 10920 cgcgaccgag ccgagcgcgt cgcccagcac ctccaggtac gcgccccgca gattgaggct 10980 cttctccttg gcgtcccgca gcagccacag gcccaccagg ttggcggcga gcccgcccag 11040 cgcgaccacg aacatcaggc cgcccttcac ctccaccggc tcgctgaacc ggccgatcgc 11100 cgaccacagg acccaggcga agatgacgac caggagcagc gcgttcagga ccgcggagaa 11160 gatctccacg cggtagaacc caaaggtgcg ccgcggcgtc ggcgcccgct gggcgagggt 11220 gatggcaccg agggccagcg agacgccgac cgcgtcggtc aggctgtgcg cggcgtcggc 11280 gagcagcgcg aggctgccgg acaggagcgc gccgaccacc tggatgacgg tgatcgagcc 11340 gctgatgccg atggtccaca gcaggcgctt gcggtacgtg ccgctgagag tgccgcccgc 11400 cgccccggcg gacggaccgt ggtcgtgccc catgcccgcg agtggaccac ggcggcgcgg 11460 cacccgccac cgagcggccg ccggtcggct cagtgcagcc gggcctgggt ggaggtgtcg 11520 cgctggtgcg ggatgccgag cggcggcggc agctcgccct gctgcaccct gaccgtgcgc 11580 acgggggcgg ggacccggat gccctcggcg cggtaacgct ggtgcaggcg cttgatgaac 11640 tcgtgcttga tgcggtactg gtcgctgaac tcgccgacgc cgaggatcac cgtgaagctg 11700 atccgcgagt cgccgaaggt gtggaagcgg atcgccgcct cgtggtcggg gaccgcgccg 11760 gtgatctcgg ccatcacctc gtccaccacc tcggtcgtga ccttctcgac ctgctccagg 11820 tcgctgtcgt agctgacccc gacctgcacc atgatcgaca gctcctgctc ggggcggctg 11880 tagttggtca tgttggtgcc ggcgagcttc gcgttgggga tgatgacgag gttgttggag 11940 agctggcgga ccgtggtgtt gcgccagttg atgtcgacga cgtagccctc ctccccgctg 12000 ctgagctgga tgtagtcgcc gggctgcacg gtcttcgcgg cgaggatgtg cacgcccgcg 12060 aagagattgg cgagcgtgtc ctgcagtgcg agggcgaccg cgagacctcc cacgccgagg 12120 gcggtgagca gcggtgcgat ggagatgccg agggtctgaa ggacgatgag gaagcccatc 12180 gcgagcacca cgacgcgggt gatgttcacg aagatggtgg ccgatccggc cactccggag 12240 cgggactgtg ccacggcctt caccaggccg gtgacgatcc gggccgccgt gagcgtggcg 12300 gccaggatga gcagcgcggt cagcgtcatg gtgacgttgc gtccggtgcg cggcgtgagc 12360 ggcagcgcgc ccgccgcggc ggcgagcccg gcggtgatgg ccgcgcaggg cacgagggtg 12420 cgcagggcgt cgacgatgac gtcgtcaccg ctccaccggg ttttgctcgc ccgttcgccg 12480 agccacctca gaagtgcgcg gagcagcagc ccggcgacga cgccggcgac gaccgcgata 12540 ccggccacga tccagtcgtg cagtgtgagg gcacgggtca tcagttcgct cccgtcgtac 12600 ggggggagtg cgcctgtgtg gggcgtatgt gatgtgacgt caccttgtga tacctgctcg 12660 attccgggga gtgcggtcac gccgggacga gagctcggtt ccggcgcgga cgtcatcctg 12720 ccccatccgc ccacggcagg cgtgcatacc cccacctgga tcttcacaga ccggccacgt 12780 ctgtccatgc gccgatgagc gcgctgcccg tggtaaagca ttgagtcagg cgatttggcc 12840 actcggcact cggcggaccg gtcgagccgg tcgatctacg tgagcggagg cggttgagca 12900 tggcgtccat gtgcagaccc ggaatgtcac ccgtcaattc gcacaacgag tgggatccgc 12960 tggaggagat catcgtcggg cggctggagg gcgcgaccat tccctccagc catccggtcg 13020 tggcgtgcaa catcccgacc tgggcggcac ggctgcaggg tctcgccgcc gggttcgagt 13080 atccgcagcg gctgatcgag ccggcgcagc aggagctcga ccagttcatc gctctcctgc 13140 aatccctcga cgtcacagtg agacggccgg cggccgtcga ccacaagcac cgcttcggga 13200 cccccgactg gcagtcgcgc ggcttctgca attcctgtcc gcgggacagc atgctcgtcg 13260 tcggcgacga gatcatcgag accccgatgg cgtggccgtg ccgctgtttc gagacgcact 13320 cgtaccgcga actcctcaag gactacttcc ggcgcggcgc gcgctggacg gcggcgccgc 13380 gcccccagct caccgaggcc ctgtacgaga aggacttccg ccctcccgag gagggcgaac 13440 gatgcgctac atcctcaccg agttcgagcc ggtgttcgac gcggcggatt tcgtgcgggc 13500 gggccgcgac ctgttcgtga cgcggagcaa cgtcgccaac ctgctgggca tcgagtggct 13560 gcgccgccac cttcgggccg gagtaccgcg tgccacgaga 13600 5 346 PRT Streptomyces cinnamonensis 5 Leu Thr Thr Arg Pro Asp Thr Lys Thr Ala Leu Ser Gln Lys Thr Ala 1 5 10 15 Leu Ser Gln Leu Leu Thr Glu Ile Glu His Arg Asn Pro Ala Gln Pro 20 25 30 Glu Phe His Gln Ala Ala Arg Glu Val Leu Glu Thr Leu Ala Pro Val 35 40 45 Ile Ala Ala Arg Pro Glu Tyr Ala Glu Ala Gly Leu Ile Glu Arg Leu 50 55 60 Cys Glu Pro Glu Arg Gln Ile Val Phe Arg Val Pro Trp Gln Asp Asp 65 70 75 80 His Gly Arg Val Arg Val Asn Arg Gly Phe Arg Val Glu Phe Asn Ser 85 90 95 Ala Leu Gly Pro Tyr Lys Gly Gly Leu Arg Phe His Pro Ser Val Asn 100 105 110 Leu Gly Val Ile Lys Phe Leu Gly Phe Glu Gln Ile Phe Lys Asn Ala 115 120 125 Leu Thr Gly Leu Gly Ile Gly Gly Gly Lys Gly Gly Ser Asp Phe Asp 130 135 140 Pro Arg Gly Arg Ser Asp Ala Glu Val Met Arg Phe Cys Gln Ser Phe 145 150 155 160 Met Thr Glu Leu Tyr Arg His Ile Gly Glu His Thr Asp Val Pro Ala 165 170 175 Gly Asp Ile Gly Val Gly Gly Arg Glu Ile Gly Tyr Leu Phe Gly Gln 180 185 190 Tyr Arg Arg Ile Thr Asn Arg Trp Glu Ala Gly Val Leu Thr Gly Lys 195 200 205 Gly Arg Asn Trp Gly Gly Ser Leu Ile Arg Pro Glu Ala Thr Gly Tyr 210 215 220 Gly Asn Val Leu Phe Ala Ala Ala Met Leu Arg Glu Arg Gly Glu Thr 225 230 235 240 Leu Glu Gly Arg Thr Ala Val Val Ser Gly Ser Gly Asn Val Ala Ile 245 250 255 Tyr Thr Ile Gln Lys Leu Ala Ala Leu Gly Ala Asn Ala Val Thr Cys 260 265 270 Ser Asp Ser Ser Gly Tyr Val Val Asp Glu Lys Gly Ile Asp Leu Asp 275 280 285 Leu Leu Lys Gln Val Lys Glu Val Glu Arg Ala Arg Val Asp Thr Tyr 290 295 300 Ala Gln Arg Arg Gly Ala Ser Ala Arg Phe Val Pro Gly Arg Arg Val 305 310 315 320 Trp Glu Val Pro Ala Asp Ile Ala Leu Pro Ser Ala Thr Gln Asn Glu 325 330 335 Leu Asp Ala Asp Asp Ala Thr Ala Leu Ile 340 345 6 306 PRT Streptomyces cinnamonensis 6 Met Thr Leu Ala Ser Ser Leu Glu Pro Thr Thr Glu Pro Leu Phe Asn 1 5 10 15 Gly Leu Tyr Val Pro Leu Val Thr Pro Phe Thr Asp Asp Leu Arg Leu 20 25 30 Ala Pro Glu Ala Leu Ala Arg Leu Ala Asp Glu Ala Leu Ser Ala Gly 35 40 45 Ala Ser Gly Leu Val Ala Leu Gly Thr Thr Ala Glu Ala Ala Thr Leu 50 55 60 Thr Ala Glu Glu Arg Glu Thr Val Ile Arg Val Cys Ser Ala Ala Cys 65 70 75 80 Arg Ala His Gly Ala Pro Leu Ile Val Gly Val Gly Thr Asn Asp Thr 85 90 95 Ala Thr Ala Ile Thr Ala Leu Arg Glu Leu Ala Ala Arg Gly Asp Val 100 105 110 Ala Ala Ala Leu Val Pro Ala Pro Pro Tyr Ile Arg Pro Gly Glu Ala 115 120 125 Gly Thr Leu Ala His Phe Ala Ala Leu Ala Glu His Gly Gly Leu Pro 130 135 140 Leu Val Val Tyr Asp Ile Pro Tyr Arg Thr Gly Gln Thr Leu Gly Ala 145 150 155 160 Gly Thr Ile Thr Ala Leu Gly Arg Leu Pro Glu Val Val Gly Ile Lys 165 170 175 His Ala Thr Gly Ser Ile Asp Pro Thr Thr Met Glu Leu Leu Asp Ser 180 185 190 Pro Leu Pro Gly Phe Ala Val Leu Gly Gly Asp Asp Ile Val Leu Ser 195 200 205 Pro Leu Val Ala Ala Gly Ala His Gly Gly Ile Val Ala Ser Ala Asn 210 215 220 Leu Arg Thr Ala Asp Tyr Ala Glu Met Ile Ala Leu Trp Arg Arg Gly 225 230 235 240 Ser Ala Ala Pro Ala Arg Ala Leu Gly Ala Asp Leu Ala Arg Leu Ser 245 250 255 Ala Ala Leu Phe Thr Glu Pro Asn Pro Thr Val Ile Lys Gly Val Leu 260 265 270 His Ala Gln Asn Arg Ile Pro Ser Pro Ala Val Arg Met Pro Leu Leu 275 280 285 Ala Ala Ser Ala Asp Ser Val Arg Arg Ala Ala Pro Leu Ala Ala Ser 290 295 300 Arg Lys 305 7 313 PRT Streptomyces cinnamonensis 7 Met Leu Asp Val Arg Arg Leu His Leu Leu Arg Glu Leu Asp Arg Arg 1 5 10 15 Gly Thr Ile Ala Ala Val Ala Glu Ala Leu Thr Phe Thr Ala Ser Ala 20 25 30 Val Ser Gln Gln Leu Gly Val Leu Glu Arg Glu Ala Gly Val Pro Leu 35 40 45 Leu Glu Arg Ser Gly Arg Arg Val Val Leu Thr Pro Ala Gly Arg Ser 50 55 60 Leu Val Ala His Ala Asp Ala Val Leu Asn Arg Leu Glu Gln Ala Val 65 70 75 80 Ala Glu Leu Ala Gly Ala Arg Asp Gly Ile Gly Gly Pro Leu Arg Ile 85 90 95 Gly Thr Phe Pro Ser Gly Gly His Thr Ile Val Pro Gly Ala Leu Ala 100 105 110 Glu Leu Ala Ser Arg His Pro Ala Leu Glu Pro Met Val Arg Glu Ile 115 120 125 Asp Ser Ala Arg Val Ser Asp Gly Leu Arg Ala Gly Glu Leu Asp Val 130 135 140 Ala Leu Val His Asp Tyr Asp Phe Val Pro Ala Thr Pro Asp Thr Thr 145 150 155 160 Val Asp Glu Val Pro Leu Leu Glu Glu Pro Met Tyr Leu Val Thr His 165 170 175 Ala Ala Asp Thr Ala Thr Asp Ser Gly Ser Gly Ser Thr Leu Ala Ala 180 185 190 Leu Leu Gly Pro Cys Ala Glu Val Pro Trp Ile Thr Ala Arg Asp Gly 195 200 205 Thr Thr Gly His Ala Met Ala Val Arg Ala Cys Gln Ala Ala Gly Phe 210 215 220 Gln Pro Arg Ile Arg His Gln Val Asn Asp Phe Arg Thr Val Leu Ala 225 230 235 240 Leu Val Ala Ala Gly Gln Gly Ala Gly Phe Val Pro Arg Met Ala Ala 245 250 255 Glu Pro Ser Pro Ala Gly Val Val Leu Thr Lys Leu Pro Leu Phe Arg 260 265 270 Arg Ser Lys Val Ala Phe Arg Ala Gly Gly Gly Ala His Pro Ala Ile 275 280 285 Ala Ala Phe Val Ala Ala Ala Thr Thr Ala Val Glu Arg Met Ala Gly 290 295 300 Ser Arg Gly Pro Ala Gly Gly Ser Glu 305 310 8 138 PRT Streptomyces cinnamonensis 8 Met Ala Asp Asp Ala Tyr Leu Phe Leu Leu Pro Asp Arg His Pro Arg 1 5 10 15 Leu Gly Ala Ala Leu Ala Ala Val Gly Ala Leu Glu Cys Thr Glu Thr 20 25 30 Pro Ala Val His Ala Trp Leu Gln Ala His Glu Ala Ser Val Ser Ser 35 40 45 Glu Gln Val Arg Ile Leu Pro Ala Asp Ala Glu Thr Leu Ile Pro Lys 50 55 60 Asp Ala Glu Arg Leu Pro Val Pro Leu Ser Glu Glu Glu Ala Leu Lys 65 70 75 80 Val Glu Gln Glu Cys Ala Pro Gln Thr Val Thr Asp Met Glu Ser Glu 85 90 95 Leu Leu Ala Phe Arg Glu Thr Thr Gln Asp Trp Gln Ala Leu Val His 100 105 110 Arg Ala Leu Thr Ala Gly Ile Pro Ala Gln Arg Ile Ala Arg Leu Thr 115 120 125 Gly Leu Asp Pro Glu Glu Ile Gly Arg Leu 130 135 9 207 PRT Streptomyces cinnamonensis 9 Leu Ala Val Ala Ala Cys Ala Ala Val Val Leu Pro Ile Asp Ala Val 1 5 10 15 Val Arg Ile Ser Ala Ala Asp Val Gly Val Leu Val Phe Phe Ala Tyr 20 25 30 Leu Leu Pro Tyr Leu Ala Ile Thr Met Thr Val Phe Val Ser Val Ala 35 40 45 Pro Glu Gln Val Arg Ser Trp Ala Arg Arg Glu Ala Arg Gly Thr Phe 50 55 60 Leu Gln Arg Tyr Val Leu Gly Thr Ala Pro Gly Pro Gly Gly Ser Leu 65 70 75 80 Phe Ile Ala Ala Ala Ala Leu Val Val Ala Val Leu Trp Leu Pro Gly 85 90 95 His Leu Ser Thr Thr Phe Ser Ala Leu Pro Arg Thr Leu Val Ala Leu 100 105 110 Ala Leu Val Val Ala Ala Trp Ile Cys Val Val Val Ala Phe Ala Val 115 120 125 Thr Phe Gln Ala Asp Asn Leu Val Glu Asn Glu Arg Ala Leu Glu Phe 130 135 140 Pro Gly Glu Arg Ser Pro Ala Trp Ala Asp Tyr Val Tyr Phe Ala Leu 145 150 155 160 Ala Ala Met Thr Thr Phe Gly Thr Thr Asp Val Asp Val Thr Ser Arg 165 170 175 Asp Met Arg Arg Thr Val Ala Ala Asn Thr Val Ile Ala Phe Val Phe 180 185 190 Asn Thr Val Thr Val Ala Ile Leu Val Ser Ala Leu Gly Gly Arg 195 200 205 10 62 PRT Streptomyces cinnamonensis 10 Met Thr Val Met Asp Lys Leu Lys Gln Met Leu Lys Gly His Glu Asp 1 5 10 15 Lys Ala Gly Gln Gly Ile Asp Lys Ala Gly Asp Phe Val Asp Gly Lys 20 25 30 Thr Gln Gly Lys Tyr Ser Gly Gln Val Asp Thr Ala Gln Asp Lys Leu 35 40 45 Arg Asp Gln Phe Gly Ser Asp Gln Gln Glu Pro Pro Gln Arg 50 55 60 11 184 PRT Streptomyces cinnamonensis 11 Met Gly Thr Ala Gln Ser Gln Glu Gln Ala Ala Ala Pro Gly Ala Cys 1 5 10 15 Ala Ala Phe Val Arg Phe Val Leu Cys Gly Gly Gly Val Gly Leu Ala 20 25 30 Ser Ser Phe Ala Val Val Ala Leu Ala Ser Trp Val Pro Trp Ala Leu 35 40 45 Ala Asn Ala Leu Val Ala Val Val Ser Thr Val Val Ala Thr Glu Leu 50 55 60 His Ala Arg Phe Thr Phe Gly Ala Gly Gly Arg Ala Thr Trp Arg Gln 65 70 75 80 His Ala Gln Ser Ala Gly Ser Ala Ala Ala Ala Tyr Ala Val Thr Cys 85 90 95 Val Ala Met Phe Val Leu Gln Gln Leu Val Ala Ala Pro Gly Ala Val 100 105 110 Leu Glu Gln Val Val Tyr Leu Ser Ala Ser Ala Leu Ala Gly Val Ala 115 120 125 Arg Phe Val Val Leu Arg Leu Val Val Phe Ala Arg Asn Arg Ser Leu 130 135 140 Pro Ala Ala Ala Ala Val Arg Thr Ala Arg Pro Val Arg Arg Val Pro 145 150 155 160 Ala Pro Val Pro Ala Thr Val Ala His Ala Ala Ser Arg Pro Ala Gly 165 170 175 Pro Ala Ala Leu Cys Pro Ala Ala 180 12 105 PRT Streptomyces cinnamonensis 12 Met Thr Ser Thr Asp His Thr Ser Gly Gln Asp Ala Thr Glu Leu Glu 1 5 10 15 Lys Gln Leu Ala Ala Ala Thr Pro Glu Glu Arg Glu Lys Leu Leu Thr 20 25 30 Asp Thr Ile Arg Thr Gln Ala Gly Thr Leu Leu Asn Thr Thr Leu Ser 35 40 45 Asp Asp Ser Asn Phe Leu Glu Asn Gly Leu Asn Ser Leu Thr Ala Leu 50 55 60 Glu Leu Thr Lys Thr Leu Met Thr Leu Thr Gly Met Glu Ile Ala Met 65 70 75 80 Val Ala Ile Val Glu Asn Pro Thr Pro Ala Gln Leu Ala His His Leu 85 90 95 Gly Gln Glu Leu Ala His Thr Thr Ala 100 105 13 828 PRT Streptomyces cinnamonensis 13 Val Ala Asn Glu Glu Lys Leu Val Glu Tyr Leu Lys Trp Thr Thr Ala 1 5 10 15 Glu Leu His Gln Ala Gln Gln Gln Leu Arg Glu Leu Lys Ala Ala Gln 20 25 30 His Glu Pro Ile Ala Val Val Ser Met Ala Cys Arg Leu Pro Gly Lys 35 40 45 Thr Arg Thr Pro Asp Asp Leu Trp Asp Leu Val Ser Glu Gly Arg Asp 50 55 60 Ala Val Thr Gly Phe Pro Asp Asp Arg Ala Trp Glu Leu Pro Glu Glu 65 70 75 80 Arg Pro Tyr Ala Glu Leu Gly Gly Phe Leu Asp Asp Ala Ala Gly Phe 85 90 95 Asp Ala Gly Phe Phe Asp Ile Ser Asp Thr Glu Ala Val Ala Thr Glu 100 105 110 Pro Leu Gln Arg Leu Met Leu His Leu Ala Trp Glu Thr Val Glu Arg 115 120 125 Gly His Ile Ala Pro His Thr Leu Arg Ser Thr Leu Thr Gly Val Tyr 130 135 140 Val Gly Ala Thr Gly His Asp Tyr Ala Thr Arg Leu Glu Thr Ala Pro 145 150 155 160 Asp Glu Leu Leu Pro Tyr Leu Gly Gly Gly Thr Ser Gly Ser Leu Val 165 170 175 Ser Gly Arg Ile Ala Tyr Ala Leu Gly Leu Glu Gly Pro Ala Ile Ser 180 185 190 Val Asp Thr Ala Cys Ser Ser Ser Leu Val Ala Leu His Leu Ala Cys 195 200 205 Gln Ala Leu Arg Arg Gly Glu Cys Gly Leu Ala Leu Ala Gly Gly Gly 210 215 220 Thr Val Met Ser Thr Pro His Thr Phe His Ala Phe Ala His Gln Lys 225 230 235 240 Ser Leu Ala Gln Asp Gly Arg Cys Lys Pro Phe Ala Ala Ala Ala Asp 245 250 255 Gly Met Gly Leu Gly Glu Gly Val Gly Leu Val Leu Leu Glu Arg Leu 260 265 270 Gly Asp Ala Arg Lys Asn Gly His Pro Val Leu Ala Val Ile Arg Gly 275 280 285 Ser Ala Val Asn Gln Asp Gly Ala Gly Tyr Gly Leu Ala Ala Pro Asn 290 295 300 Gly Pro Ser Gln Gln His Val Ile Arg Ala Ala Leu Ala Asp Ala Gly 305 310 315 320 Leu Thr Pro Asp Gln Ile Asp Ala Val Glu Ala His Gly Thr Gly Thr 325 330 335 Pro Ile Gly Asp Ala Ile Glu Val Gln Ala Leu Leu Ala Thr Tyr Gly 340 345 350 Ala Asp Arg Ser Pro Asp Arg Pro Leu Trp Leu Gly Ser Val Lys Ser 355 360 365 Asn Thr Gly His Thr Gln Gly Ala Ala Gly Ala Ala Ala Leu Ile Lys 370 375 380 Met Val Gln Ala Phe Arg His Gly Thr Leu Pro Pro Thr Leu His Val 385 390 395 400 Asp Arg Pro Thr Pro Leu Ala Ala Trp Lys Lys Gly Ala Val Arg Leu 405 410 415 Leu Thr Glu Ala Val Asp Trp Pro Arg Arg Glu Glu Pro Arg Arg Val 420 425 430 Gly Ile Ser Ala Phe Ala Thr Ser Gly Thr Asn Ala His Leu Ile Leu 435 440 445 Glu Glu Pro Pro Val Asp Glu Ala Pro Val Pro Asp Ala Ala Arg Asp 450 455 460 Gln Thr Ser Pro Val Ala Pro Glu Leu Pro Val Ala Trp Ser Leu Ser 465 470 475 480 Ala Arg Thr Pro Glu Ala Leu Arg Ala Gln Ala Lys Ala Leu Val Thr 485 490 495 His Leu Ala Ala Thr Asp Pro Ala Pro Ser Pro Ala Glu Val Ala Tyr 500 505 510 Ser Leu Ala Ala Thr Arg Ser Pro Leu Glu His Arg Ala Val Leu Thr 515 520 525 Gly Thr Asp His Thr Glu Leu Leu Ala Ala Ala Arg Ala Leu Ala Ala 530 535 540 Gly Glu Asp His Pro Asp Leu Val Arg Ser Thr Pro Gly Ala Gly Pro 545 550 555 560 Lys Lys Ile Ala Trp His Phe Asp Gly Arg Pro Ala Asp Gly Val Thr 565 570 575 Thr Gly Ala Ala Pro Gly Ala Lys Pro Gly Ala Thr Phe Gly Ala Thr 580 585 590 Phe Gly Ala Ala Phe Gly Gly Ala Glu Phe His Ser Ala Phe Pro Leu 595 600 605 Phe Ala Ser Ala Phe Asp Glu Ala Arg Ala Leu Leu Asp Thr His Leu 610 615 620 Pro Thr Pro Leu Pro Thr Pro His Ser Glu Leu Ala Arg Phe Ala Val 625 630 635 640 His Thr Ala Leu Ala Arg Leu Leu Leu Glu Thr Gly Val Arg Pro His 645 650 655 Thr Leu Thr Gly Asp Gly Val Gly His Ile Ala Ala Ala Tyr Ala Ala 660 665 670 Gly Ile Leu Thr Leu Asp Asp Ala Cys Arg Leu Ala Ala Ala His Ala 675 680 685 Ala Ala Ala Gln Ala Ala Glu Gly Glu Gln Pro Ala Pro Pro Asp Ala 690 695 700 Tyr Glu Pro Val Leu Lys Gln Leu Thr Phe Gln Arg Ala Thr Leu Thr 705 710 715 720 Leu Thr Ser Thr Ala Pro Ala Asp Thr Pro Ile Ala Ser Ala Asp Tyr 725 730 735 Trp His His His Leu Thr Ser Pro Ala Pro Thr Ala Pro Pro Thr Pro 740 745 750 Glu Thr His Thr Leu Leu His Leu Gly Ala Leu Ser Pro Glu Gly Thr 755 760 765 Gln Thr Ser Ala Val Ser Ala Leu Leu Thr Ala Leu Ala Arg Leu His 770 775 780 Thr Thr Gly Gly Thr Val Asp Trp Thr Pro Leu Val Arg Arg Thr Pro 785 790 795 800 His Pro Arg Thr Ile Asp Leu Pro Thr Tyr Ser Phe Gln Ala Thr Arg 805 810 815 Tyr Trp Leu His Asp His Thr Ala His Ala Ala Val 820 825 14 299 PRT Streptomyces cinnamonensis 14 Val Lys Asn Leu Arg Ile Pro Val Ser Gln Thr Val Ser Leu Asn Val 1 5 10 15 Arg Tyr Arg Pro Ala Asp Gly Pro Gly Ala Pro Gly Arg Pro Phe Leu 20 25 30 Leu Leu His Gly Met Leu Ser Asn Ala Arg Met Trp Asp Glu Val Ala 35 40 45 Ala Arg Leu Ala Ala Ala Gly His Pro Ala Tyr Ala Val Asp His Arg 50 55 60 Gly His Gly Glu Ser Asp Thr Pro Pro Asp Gly Tyr Asp Asn Ala Thr 65 70 75 80 Val Val Thr Asp Leu Val Ala Ala Val Thr Ala Leu Asp Leu Ser Gly 85 90 95 Ala Leu Val Ala Gly His Ser Trp Gly Ala His Leu Ala Leu Arg Leu 100 105 110 Ala Ala Glu His Pro Asp Leu Val Ala Gly Leu Ala Leu Ile Asp Gly 115 120 125 Gly Trp Tyr Glu Phe Asp Gly Pro Val Met Arg Ala Phe Trp Glu Arg 130 135 140 Thr Ala Asp Val Val Arg Arg Ala Gln Gln Gly Thr Thr Ser Ala Ala 145 150 155 160 Asp Met Arg Ala Tyr Leu Arg Ala Thr His Pro Asp Trp Ser Pro Thr 165 170 175 Ser Ile Glu Ala Arg Leu Ala Asp Tyr Arg Val Gly Pro Asp Gly Leu 180 185 190 Leu Ile Pro Arg Leu Thr Ser Thr Gln Val Met Ser Ile Val Ala Gly 195 200 205 Leu Gln Arg Glu Ala Pro Ala Asp Trp Tyr Pro Lys Val Thr Val Pro 210 215 220 Val Arg Leu Leu Pro Leu Ile Pro Ala Ile Pro Gln Leu Ser Asp Gln 225 230 235 240 Val Arg Ala Trp Val Ala Ala Ala Glu Ala Ala Leu Glu Gln Val Ser 245 250 255 Val Arg Trp Tyr Pro Gly Ser Asp His Asp Leu His Ala Gly Ala Pro 260 265 270 Asp Glu Ile Ala Ala Asp Leu Leu Leu Leu Ala Arg Ser Cys Glu Ala 275 280 285 Met Pro Gly Gly Lys Ala Gly Val Arg Pro Ala 290 295 15 276 PRT Streptomyces cinnamonensis 15 Val Asn Lys Thr Val Ala Pro Glu Pro Ser Asp Ile Gly His Tyr Tyr 1 5 10 15 Asp His Lys Val Phe Asp Leu Met Thr Gln Leu Gly Asp Gly Asn Leu 20 25 30 His Tyr Gly Tyr Trp Phe Asp Gly Gly Glu Gln Gln Ala Thr Phe Asp 35 40 45 Glu Ala Met Val Gln Met Thr Asp Glu Met Ile Arg Arg Leu Asp Pro 50 55 60 Ala Pro Gly Asp Arg Val Leu Asp Ile Gly Cys Gly Asn Gly Thr Pro 65 70 75 80 Ala Met Gln Leu Ala Arg Ala Arg Asp Val Glu Val Val Gly Ile Ser 85 90 95 Val Ser Ala Arg Gln Val Glu Arg Gly Asn Arg Arg Ala Arg Glu Ala 100 105 110 Gly Leu Ala Asp Arg Val Arg Phe Glu Gln Val Asp Ala Met Asn Leu 115 120 125 Pro Phe Asp Asp Gly Ser Phe Asp His Cys Trp Ala Leu Glu Ser Met 130 135 140 Leu His Met Pro Asp Lys Gln Gln Val Leu Thr Glu Ala His Arg Val 145 150 155 160 Val Lys Pro Gly Ala Arg Met Pro Ile Ala Asp Met Val Tyr Leu Asn 165 170 175 Pro Asp Pro Ser Arg Pro Arg Thr Ala Thr Val Ser Asp Thr Thr Ile 180 185 190 Tyr Ala Ala Leu Thr Asp Ile Gly Asp Tyr Pro Asp Ile Phe Arg Ala 195 200 205 Ala Gly Trp Thr Val Leu Glu Leu Thr Asp Ile Thr Arg Glu Thr Ala 210 215 220 Lys Thr Tyr Asp Gly Tyr Val Glu Trp Ile Arg Ala His Arg Asp Glu 225 230 235 240 Tyr Val Asp Ile Ile Gly Val Glu Gly Tyr Glu Leu Phe Leu His Asn 245 250 255 Gln Ala Ala Leu Gly Lys Met Pro Glu Leu Gly Tyr Ile Phe Ala Thr 260 265 270 Ala Gln Arg Pro 275 16 511 PRT Streptomyces cinnamonensis 16 Met Ser Ala Asp Leu Gly Ala Arg Arg Trp Trp Ala Val Gly Ala Leu 1 5 10 15 Val Leu Ala Ser Met Val Val Gly Phe Asp Val Thr Ile Leu Ser Leu 20 25 30 Ala Leu Pro Ala Met Ala Asp Asp Leu Gly Ala Asn Asn Val Glu Leu 35 40 45 Gln Trp Phe Val Thr Ser Tyr Thr Leu Val Phe Ala Ala Gly Met Ile 50 55 60 Pro Ala Gly Met Leu Gly Asp Arg Phe Gly Arg Lys Lys Val Leu Leu 65 70 75 80 Thr Ala Leu Val Ile Phe Gly Ile Ala Ser Leu Ala Cys Ala Tyr Ala 85 90 95 Thr Ser Ser Gly Thr Phe Ile Gly Ala Arg Ala Val Leu Gly Leu Gly 100 105 110 Ala Ala Leu Ile Met Pro Thr Thr Leu Ser Leu Leu Pro Val Met Phe 115 120 125 Ser Asp Glu Glu Arg Pro Lys Ala Ile Gly Ala Val Ala Gly Ala Ala 130 135 140 Met Leu Ala Tyr Pro Leu Gly Pro Ile Leu Gly Gly Tyr Leu Leu Asn 145 150 155 160 His Phe Trp Trp Gly Ser Val Phe Leu Ile Asn Val Pro Val Val Ile 165 170 175 Leu Ala Phe Leu Ala Val Ser Ala Trp Leu Pro Glu Ser Lys Ala Lys 180 185 190 Glu Ala Lys Pro Phe Asp Ile Gly Gly Leu Val Phe Ser Ser Val Gly 195 200 205 Leu Ala Ala Leu Thr Tyr Gly Val Ile Gln Gly Gly Glu Lys Gly Trp 210 215 220 Thr Asp Val Thr Thr Leu Val Pro Cys Ile Gly Gly Leu Leu Ala Leu 225 230 235 240 Val Leu Phe Val Met Trp Glu Lys Arg Val Ala Asp Pro Leu Val Asp 245 250 255 Leu Ser Leu Phe Arg Ser Ala Arg Phe Thr Ser Gly Thr Met Leu Gly 260 265 270 Thr Val Ile Asn Phe Thr Met Phe Gly Val Leu Phe Thr Met Pro Gln 275 280 285 Tyr Tyr Gln Ala Val Leu Gly Thr Asp Ala Met Gly Ser Gly Phe Arg 290 295 300 Leu Leu Pro Met Val Gly Gly Leu Leu Val Gly Val Thr Val Ala Asn 305 310 315 320 Lys Val Ala Lys Ala Leu Gly Pro Lys Thr Ala Val Gly Ile Gly Phe 325 330 335 Ala Leu Leu Ala Ala Ala Leu Phe Tyr Gly Ala Thr Thr Asp Val Ser 340 345 350 Ser Gly Thr Gly Leu Ala Ala Ala Trp Thr Ala Ala Tyr Gly Leu Gly 355 360 365 Leu Gly Ile Ala Leu Pro Thr Ala Met Asp Ala Ala Leu Gly Ala Leu 370 375 380 Ser Glu Asp Ser Ala Gly Val Gly Ser Gly Val Asn Gln Ser Ile Arg 385 390 395 400 Thr Leu Gly Gly Ser Phe Gly Ala Ala Ile Leu Gly Ser Ile Leu Asn 405 410 415 Ser Gly Tyr Arg Gly Lys Leu Asp Leu Asp Gly Val Pro Glu Gln Ala 420 425 430 His Gly Ala Val Lys Asp Ser Val Phe Gly Gly Leu Ala Val Ala Arg 435 440 445 Ala Ile Lys Ser Asn Gly Leu Ala Asp Ser Val Arg Ser Ala Tyr Val 450 455 460 His Ala Leu Asp Val Val Leu Val Val Ser Gly Gly Leu Gly Leu Leu 465 470 475 480 Gly Val Val Leu Ala Val Val Trp Leu Pro Arg His Val Gly Gln Ser 485 490 495 Thr Ala Lys Thr Ala Glu Ser Glu His Glu Ala Ala Asp Ala Val 500 505 510 17 191 PRT Streptomyces cinnamonensis 17 Val Pro Gly Leu Arg Glu Arg Lys Lys Ala Arg Thr Lys Ala Ala Ile 1 5 10 15 Gln Arg Glu Ala Val Arg Leu Phe Arg Glu Gln Gly Tyr Thr Ala Thr 20 25 30 Thr Ile Glu Gln Ile Ala Glu Ala Ala Glu Val Ala Pro Ser Thr Val 35 40 45 Phe Arg Tyr Phe Ala Thr Lys Gln Asp Leu Val Phe Ser His Asp Tyr 50 55 60 Asp Leu Pro Phe Ala Met Met Val Gln Ala Gln Ser Pro Asp Leu Thr 65 70 75 80 Pro Ile Gln Ala Glu Arg Gln Ala Ile Arg Ser Met Leu Gln Asp Ile 85 90 95 Ser Glu Gln Glu Leu Ala Leu Gln Arg Glu Arg Phe Val Leu Ile Leu 100 105 110 Ser Glu Pro Glu Leu Trp Gly Ala Ser Leu Gly Asn Ile Gly Gln Thr 115 120 125 Met Gln Ile Met Ser Glu Gln Val Ala Lys Arg Ala Gly Arg Asp Pro 130 135 140 Arg Asp Pro Ala Val Arg Ala Tyr Thr Gly Ala Val Phe Gly Val Met 145 150 155 160 Leu Gln Val Ser Met Asp Trp Ala Asn Asp Pro Asp Met Asp Phe Ala 165 170 175 Thr Thr Leu Asp Glu Ala Leu His Tyr Leu Glu Asp Leu Arg Pro 180 185 190 18 268 PRT Streptomyces cinnamonensis 18 Met Asp Arg Gly Thr Ala Ala Arg Ala Pro Gln Ile Gly Asp Glu Phe 1 5 10 15 Gly Ala Ala Thr Gly Asn Gly Val Trp Leu Arg Arg Tyr His Ala Ala 20 25 30 Ala Glu Ala Pro Val Arg Leu Val Cys Phe Pro Phe Ala Gly Gly Ser 35 40 45 Ala Ser Tyr Tyr Phe Gly Leu Ser Gly Leu Leu Ala Pro Gly Val Glu 50 55 60 Val Leu Ala Val Gln Tyr Pro Gly Arg Gln Asp Arg His Ala Glu Pro 65 70 75 80 Cys Leu Ala Ser Val Ala Glu Leu Ala Asp Gly Val Val Pro His Leu 85 90 95 Pro Cys Asp Gly Lys Pro Phe Ala Leu Phe Gly His Ser Leu Gly Ala 100 105 110 Ile Val Ala Phe Glu Val Ala Arg Arg Leu Arg Gly Pro Ala Gly Pro 115 120 125 Gly Leu Pro Val His Leu Phe Val Ser Gly Gly Leu Ala Arg Pro Tyr 130 135 140 Arg Pro Ala Gly Arg Ser Gly Ala Phe Gly Asp Ala Asp Ile Leu Ala 145 150 155 160 His Leu Arg Ala Met Gly Gly Thr Asp Glu Arg Phe Phe Arg Ser Pro 165 170 175 Glu Leu Gln Glu Leu Val Leu Pro Ala Leu Arg Ala Asp Tyr Arg Ala 180 185 190 Val Ala Thr Tyr Glu Ala Pro Gly Pro Gly Arg Leu Asp Cys Pro Ile 195 200 205 Thr Ala Leu Ile Gly Asp Ala Asp Glu Arg Thr Ser Pro Glu Gln Ala 210 215 220 Ala Thr Trp Arg Glu Arg Thr Gly Ala Ala Phe Asp Leu Arg Val Leu 225 230 235 240 Pro Gly Gly His Phe Tyr Leu Asp Gly Cys Gln Glu Gln Val Ala Ala 245 250 255 Val Val Thr Glu Ala Leu Thr Ala Gly Pro Gly Val 260 265 19 3025 PRT Streptomyces cinnamonensis 19 Met Ala Ala Ser Ala Ser Ala Ser Pro Ser Gly Pro Ser Ala Gly Pro 1 5 10 15 Asp Pro Ile Ala Val Val Gly Met Ala Cys Arg Leu Pro Gly Ala Pro 20 25 30 Asp Pro Asp Ala Phe Trp Arg Leu Leu Ser Glu Gly Arg Ser Ala Val 35 40 45 Ser Thr Ala Pro Pro Glu Arg Arg Arg Ala Asp Ser Gly Leu His Gly 50 55 60 Pro Gly Gly Tyr Leu Asp Arg Ile Asp Gly Phe Asp Ala Asp Phe Phe 65 70 75 80 His Ile Ser Pro Arg Glu Ala Val Ala Met Asp Pro Gln Gln Arg Leu 85 90 95 Leu Leu Glu Leu Ser Trp Glu Ala Leu Glu Asp Ala Gly Ile Arg Pro 100 105 110 Pro Thr Leu Ala Arg Ser Arg Thr Gly Val Phe Val Gly Ala Phe Trp 115 120 125 Asp Asp Tyr Thr Asp Val Leu Asn Leu Arg Ala Pro Gly Ala Val Thr 130 135 140 Arg His Thr Met Thr Gly Val His Arg Ser Ile Leu Ala Asn Arg Ile 145 150 155 160 Ser Tyr Ala Tyr His Leu Ala Gly Pro Ser Leu Thr Val Asp Thr Ala 165 170 175 Gln Ser Ser Ser Leu Val Ala Val His Leu Ala Cys Glu Ser Ile Arg 180 185 190 Ser Gly Asp Ser Asp Ile Ala Phe Ala Gly Gly Val Asn Leu Ile Cys 195 200 205 Ser Pro Arg Thr Thr Glu Leu Ala Ala Ala Arg Phe Gly Gly Leu Ser 210 215 220 Ala Ala Gly Arg Cys His Thr Phe Asp Ala Arg Ala Asp Gly Phe Val 225 230 235 240 Arg Gly Glu Gly Gly Gly Leu Val Val Leu Lys Pro Leu Ala Ala Ala 245 250 255 Arg Arg Asp Gly Asp Thr Val Tyr Cys Val Ile Arg Gly Ser Ala Val 260 265 270 Asn Ser Asp Gly Thr Thr Asp Gly Ile Thr Leu Pro Ser Gly Gln Ala 275 280 285 Gln Gln Asp Val Val Arg Leu Ala Cys Arg Arg Ala Arg Ile Thr Pro 290 295 300 Asp Gln Val Gln Tyr Val Glu Leu His Gly Thr Gly Thr Pro Val Gly 305 310 315 320 Asp Pro Ile Glu Ala Ala Ala Leu Gly Ala Ala Leu Gly Gln Asp Ala 325 330 335 Ala Arg Ala Val Pro Leu Ala Val Gly Ser Ala Lys Thr Asn Val Gly 340 345 350 His Leu Glu Ala Ala Ala Gly Ile Val Gly Leu Leu Lys Thr Ala Leu 355 360 365 Ser Ile His His Arg Arg Leu Ala Pro Ser Leu Asn Phe Thr Thr Pro 370 375 380 Asn Pro Ala Ile Pro Leu Ala Asp Leu Gly Leu Thr Val Gln Gln Asp 385 390 395 400 Leu Ala Asp Trp Pro Arg Pro Glu Gln Pro Leu Ile Ala Gly Val Ser 405 410 415 Ser Phe Gly Met Gly Gly Thr Asn Gly His Val Val Val Ala Ala Ala 420 425 430 Pro Asp Ser Val Ala Val Pro Glu Pro Val Gly Val Pro Glu Arg Val 435 440 445 Glu Val Pro Glu Pro Val Val Val Ser Glu Pro Val Val Val Pro Thr 450 455 460 Pro Trp Pro Val Ser Ala His Ser Ala Ser Ala Leu Arg Ala Gln Ala 465 470 475 480 Gly Arg Leu Arg Thr His Leu Ala Ala His Arg Pro Thr Pro Asp Ala 485 490 495 Ala Arg Val Gly His Ala Leu Ala Thr Thr Arg Ala Pro Leu Ala His 500 505 510 Arg Ala Val Leu Leu Gly Gly Asp Thr Ala Glu Leu Leu Gly Ser Leu 515 520 525 Asp Ala Leu Ala Glu Gly Ala Glu Thr Ala Ser Ile Val Arg Gly Glu 530 535 540 Ala Tyr Thr Glu Gly Arg Thr Ala Phe Leu Phe Ser Gly Gln Gly Ala 545 550 555 560 Gln Arg Leu Gly Met Gly Arg Glu Leu Tyr Ala Val Phe Pro Val Phe 565 570 575 Ala Asp Ala Leu Asp Glu Ala Phe Ala Ala Leu Asp Val His Leu Asp 580 585 590 Arg Pro Leu Arg Glu Ile Val Leu Gly Glu Thr Asp Ser Gly Gly Asn 595 600 605 Val Ser Gly Glu Asn Val Ile Gly Glu Gly Ala Asp His Gln Ala Leu 610 615 620 Leu Asp Gln Thr Ala Tyr Thr Gln Pro Ala Leu Phe Ala Ile Glu Thr 625 630 635 640 Ser Leu Tyr Arg Leu Ala Ala Ser Phe Gly Leu Lys Pro Asp Tyr Val 645 650 655 Leu Gly His Ser Val Gly Glu Ile Ala Ala Ala His Val Ala Gly Val 660 665 670 Leu Ser Leu Pro Asp Ala Ser Ala Leu Val Ala Thr Arg Gly Arg Leu 675 680 685 Met Gln Ala Val Arg Ala Pro Gly Ala Met Ala Ala Trp Gln Ala Thr 690 695 700 Ala Asp Glu Ala Ala Glu Gln Leu Ala Gly His Glu Arg His Val Thr 705 710 715 720 Val Ala Ala Val Asn Gly Pro Asp Ser Val Val Val Ser Gly Asp Arg 725 730 735 Ala Thr Val Asp Glu Leu Thr Ala Ala Trp Arg Gly Arg Gly Arg Lys 740 745 750 Ala His His Leu Lys Val Ser His Ala Phe His Ser Pro His Met Asp 755 760 765 Pro Ile Leu Asp Glu Leu Arg Ala Val Ala Ala Gly Leu Thr Phe His 770 775 780 Glu Pro Val Ile Pro Val Val Ser Asn Val Thr Gly Glu Leu Val Thr 785 790 795 800 Ala Thr Ala Thr Gly Ser Gly Ala Gly Gln Ala Asp Pro Glu Tyr Trp 805 810 815 Ala Arg His Ala Arg Glu Pro Val Arg Phe Leu Ser Gly Val Arg Gly 820 825 830 Leu Cys Glu Arg Gly Val Thr Thr Phe Val Glu Leu Gly Pro Asp Ala 835 840 845 Pro Leu Ser Ala Met Ala Arg Asp Cys Phe Pro Ala Pro Ala Asp Arg 850 855 860 Ser Arg Pro Arg Pro Ala Ala Ile Ala Thr Cys Arg Arg Gly Arg Asp 865 870 875 880 Glu Val Ala Thr Phe Leu Arg Ser Leu Ala Gln Ala Tyr Val Arg Gly 885 890 895 Ala Asp Val Asp Phe Thr Arg Ala Tyr Gly Ala Thr Ala Thr Arg Arg 900 905 910 Phe Pro Leu Pro Thr Tyr Pro Phe Gln Arg Glu Arg His Trp Pro Ala 915 920 925 Ala Ala Gly Val Gly Gln Gln Pro Glu Thr Pro Glu Leu Pro Glu Ser 930 935 940 Ser Glu Ser Ser Glu Gln Ala Gly His Glu Arg Glu Glu Gly Ala Arg 945 950 955 960 Ala Trp Gly Gly Pro Glu Gly Arg Leu Ala Gly Leu Ser Val Asn Asp 965 970 975 Gln Glu Arg Val Leu Leu Gly Leu Val Thr Lys His Val Ala Val Val 980 985 990 Leu Gly Asp Ala Ser Gly Thr Val Gln Ala Ala Arg Thr Phe Lys Gln 995 1000 1005 Leu Gly Phe Asp Ser Met Ala Ala Ala Glu Leu Ser Glu Arg Leu Gly 1010 1015 1020 Thr Glu Thr Gly Leu Pro Leu Pro Ala Thr Leu Thr Phe Asp Tyr Pro 1025 1030 1035 1040 Thr Pro Leu Ala Val Ala Ala His Leu Arg Ala Glu Leu Thr Gly Thr 1045 1050 1055 Pro Ala Pro Ala Gly Ser Ala Pro Ala Thr Gly Ala Leu Gly Ala Gly 1060 1065 1070 Asp Leu Gly Thr Asp Glu Asp Pro Val Ala Ile Val Ala Met Ser Cys 1075 1080 1085 Arg Tyr Pro Gly Gly Ala Gly Thr Pro Glu Asp Leu Trp Arg Leu Val 1090 1095 1100 Ala Asp Gly Ala Asp Ala Ile Gly Asp Phe Pro Thr Asp Arg Gly Trp 1105 1110 1115 1120 Asp Leu Ala Arg Leu Phe His Pro Asp Pro Asp Arg Ser Gly Thr Ser 1125 1130 1135 Cys Thr Arg Gln Gly Gly Phe Leu Tyr Asp Ala Ala Asp Phe Asp Ala 1140 1145 1150 Glu Phe Phe Asp Ile Ser Pro Arg Glu Ala Leu Ala Val Asp Pro Gln 1155 1160 1165 Gln Arg Leu Leu Leu Glu Cys Ala Trp Glu Ala Phe Glu Arg Ala Gly 1170 1175 1180 Leu Asp Pro Arg Ala Leu Lys Gly Ser Pro Thr Gly Val Phe Val Gly 1185 1190 1195 1200 Met Thr Gly Gln Asp Tyr Gly Pro Arg Leu His Glu Pro Ser Gln Ala 1205 1210 1215 Thr Asp Gly Tyr Leu Leu Thr Gly Ser Thr Pro Ser Val Ala Ser Gly 1220 1225 1230 Arg Leu Ser Phe Ser Phe Gly Leu Glu Gly Pro Ala Leu Thr Val Asp 1235 1240 1245 Thr Ala Cys Ser Ser Ser Leu Val Thr Leu His Leu Ala Ala Gln Ala 1250 1255 1260 Leu Arg Arg Gly Glu Cys Asp Leu Ala Leu Ala Gly Gly Ala Thr Val 1265 1270 1275 1280 Leu Ala Thr Pro Gly Met Phe Thr Glu Phe Ser Arg Gln Arg Gly Leu 1285 1290 1295 Ala Pro Asp Gly Arg Cys Lys Pro Phe Ala Ala Gly Ala Asp Gly Thr 1300 1305 1310 Gly Trp Ala Glu Gly Val Gly Leu Val Leu Leu Glu Arg Leu Ser Glu 1315 1320 1325 Ala Arg Arg Lys Gly His Ala Val Leu Ala Val Ile Arg Gly Ser Ala 1330 1335 1340 Ile Asn Gln Asp Gly Ala Ser Asn Gly Leu Thr Ala Pro Asn Gly Pro 1345 1350 1355 1360 Ser Gln Gln Arg Val Ile Arg Ala Ala Leu Ala Ala Ala Arg Leu Thr 1365 1370 1375 Ala Asp Glu Val Asp Val Val Glu Ala His Gly Thr Gly Thr Thr Leu 1380 1385 1390 Gly Asp Pro Ile Glu Ala Gln Ala Leu Leu Ala Thr Tyr Gly Gln Gly 1395 1400 1405 Arg Ser Ala Glu Arg Pro Leu Trp Leu Gly Ser Val Lys Ser Asn Ile 1410 1415 1420 Gly His Thr Gln Ala Ala Ala Gly Val Ala Gly Val Ile Lys Met Val 1425 1430 1435 1440 Met Ala Met Arg His Asp Leu Leu Pro Ala Thr Leu His Val Asp Glu 1445 1450 1455 Pro Ser Gly His Val Asp Trp Ser Thr Gly Ala Val Arg Leu Leu Thr 1460 1465 1470 Glu Pro Val Val Trp Pro Arg Gly Glu Arg Pro Arg Arg Ala Ala Val 1475 1480 1485 Ser Ser Phe Gly Ile Ser Gly Thr Asn Ala His Leu Val Leu Glu Glu 1490 1495 1500 Ala Gly Gln Asp Glu Tyr Val Ala Gly Ala Ala Asp Asp Ala Gly Pro 1505 1510 1515 1520 Val Asp Gly Ala Val Leu Pro Trp Val Val Ser Gly Arg Thr Gly Ala 1525 1530 1535 Ala Leu Arg Glu Gln Ala Arg Arg Leu Arg Glu Leu Val Thr Gly Gly 1540 1545 1550 Ser Ala Asp Val Ser Val Ser Gly Val Gly Arg Ser Leu Val Thr Thr 1555 1560 1565 Arg Ala Val Phe Glu His Arg Ala Val Val Val Gly Arg Asp Arg Asp 1570 1575 1580 Thr Leu Ile Gly Gly Leu Glu Ala Leu Ala Ala Gly Asp Ala Ser Pro 1585 1590 1595 1600 Asp Val Val Cys Gly Val Ala Gly Asp Val Gly Pro Gly Pro Val Leu 1605 1610 1615 Val Phe Pro Gly Gln Gly Ser Gln Trp Val Gly Met Gly Ala Gln Leu 1620 1625 1630 Leu Gly Glu Ser Ala Val Phe Ala Ala Arg Ile Asp Ala Cys Glu Gln 1635 1640 1645 Ala Leu Ser Pro Tyr Val Asp Trp Ser Leu Thr Glu Val Leu Arg Gly 1650 1655 1660 Asp Gly Arg Glu Leu Ser Arg Val Asp Val Val Gln Pro Val Leu Trp 1665 1670 1675 1680 Ala Val Met Val Ser Leu Ala Ala Val Trp Ala Asp His Gly Val Thr 1685 1690 1695 Pro Ala Ala Val Val Gly His Ser Gln Gly Glu Ile Ala Ala Val Val 1700 1705 1710 Val Ala Gly Ala Leu Thr Leu Glu Asp Gly Ala Lys Ile Val Ala Leu 1715 1720 1725 Arg Ser Arg Ala Leu Arg Gln Leu Ser Gly Gly Gly Ala Met Ala Ser 1730 1735 1740 Leu Gly Val Gly Gln Glu Gln Ala Ala Glu Leu Val Glu Gly His Pro 1745 1750 1755 1760 Gly Val Gly Ile Ala Ala Val Asn Gly Pro Ser Ser Thr Val Ile Ser 1765 1770 1775 Gly Pro Pro Glu Gln Val Ala Ala Val Val Ala Asp Ala Glu Ala Arg 1780 1785 1790 Glu Leu Arg Gly Arg Val Ile Asp Val Asp Tyr Ala Ser His Ser Pro 1795 1800 1805 Gln Val Asp Ala Ile Thr Asp Glu Leu Thr His Thr Leu Ser Gly Val 1810 1815 1820 Arg Pro Thr Thr Ala Pro Val Ala Phe Tyr Ser Ala Val Thr Gly Thr 1825 1830 1835 1840 Arg Ile Asp Thr Ala Gly Leu Asp Thr Asp Tyr Trp Val Thr Asn Leu 1845 1850 1855 Arg Arg Pro Val Arg Phe Ala Asp Ala Val Thr Ala Leu Leu Ala Asp 1860 1865 1870 Gly His Arg Val Phe Ile Glu Ala Ser Ser His Pro Val Leu Thr Leu 1875 1880 1885 Gly Leu Gln Glu Thr Phe Glu Glu Ala Gly Val Asp Ala Val Thr Val 1890 1895 1900 Pro Thr Leu Arg Arg Glu Asp Gly Gly Arg Ala Arg Leu Ala Arg Ser 1905 1910 1915 1920 Leu Ala Gln Ala Phe Gly Ala Gly Cys Ala Val Arg Trp Glu Asn Trp 1925 1930 1935 Phe Pro Ala Thr Gly Thr Ser Thr Val Glu Leu Pro Thr Tyr Ala Phe 1940 1945 1950 Gln Arg Arg Arg Tyr Trp Leu Glu Ala Pro Thr Gly Thr Gln Asp Ala 1955 1960 1965 Ala Gly Leu Gly Leu Ala Ala Ala Gly His Pro Leu Leu Gly Ala Ala 1970 1975 1980 Thr Glu Ile Ala Asp Gly Asp Ile Arg Leu Leu Thr Gly Arg Ile Ser 1985 1990 1995 2000 Arg His Ser His Pro Trp Leu Ala Gln His Thr Leu Phe Gly Ala Ala 2005 2010 2015 Val Val Pro Ala Ser Val Leu Ala Glu Trp Ala Leu Arg Ala Ala Asp 2020 2025 2030 Glu Ala Gly Cys Pro Arg Val Asp Asp Leu Thr Leu Arg Thr Pro Leu 2035 2040 2045 Val Leu Pro Glu Thr Ala Gly Val Gln Val Gln Ile Val Val Gly Pro 2050 2055 2060 Ala Asp Ala Arg Asp Gly His Arg Asp Phe His Val Tyr Ala Arg Pro 2065 2070 2075 2080 Asp Gly Lys Asp Ala Ser Glu Gly Glu Gly Ile Ala Glu Gly Glu Gly 2085 2090 2095 Ala Ser Glu Gly Glu Gly Ala Ser Gly Gly Thr Asp Ala Pro Trp Thr 2100 2105 2110 Cys His Ala Asp Gly Arg Leu Val Ala Glu Pro Thr Gly Thr Ala Ser 2115 2120 2125 Glu Asp Ser Pro Asp Thr Val Trp Pro Pro Pro Gly Ala Glu Pro Val 2130 2135 2140 Asp Leu Gly Asp Phe Tyr Glu Arg Ala Ala Ala Thr Gly Val Gly Tyr 2145 2150 2155 2160 Gly Pro Val Phe Thr Gly Leu Arg Ala Leu Trp Arg Arg Asp Gly Glu 2165 2170 2175 Leu Phe Ala Glu Ala Val Leu Pro Gln Glu Ala Pro Glu Thr Ala Gly 2180 2185 2190 Phe Gly Met His Pro Ala Leu Leu Asp Ala Ala Leu His Pro Ala Leu 2195 2200 2205 Leu Gly Glu Arg Pro Ala Glu Glu Asp Lys Val Trp Leu Pro Phe Thr 2210 2215 2220 Leu Thr Gly Val Thr Leu Trp Ala Thr Gly Ala Thr Ser Val Arg Val 2225 2230 2235 2240 Arg Leu Thr Pro Leu Asp Asp Asp Pro Asp Ala Ser Ala Asp Gly Arg 2245 2250 2255 Ala Trp Arg Val Gly Val Ser Asp Pro Thr Gly Ala Glu Val Leu Thr 2260 2265 2270 Cys Glu Ala Leu Val Ala Val Ala Ala Gly Arg Arg Glu Leu Arg Ala 2275 2280 2285 Ala Gly Glu Arg Val Ser Asp Leu Tyr Ala Val Glu Trp Val Pro Val 2290 2295 2300 Pro Gly Pro Gly Pro Val Gly Glu Gly Ala Asp Phe Ser Gly Trp Ala 2305 2310 2315 2320 Gly Leu Gly Glu Cys Gly Glu Arg Trp Glu Cys Val Gly Arg Val Glu 2325 2330 2335 Arg Trp Tyr Glu Asp Leu Asp Ala Leu Gly Ala Ala Val Glu Gly Gly 2340 2345 2350 Ala Ser Val Pro Ser Val Val Leu Ala Thr Ala Ala Ala Ala Pro Gly 2355 2360 2365 Gly Ala Gly Asp Gly Ala Ala Asp Ala Leu Ser Ala Val Arg Trp Thr 2370 2375 2380 Gly Ala Leu Leu Asp Gln Trp Leu Ala Asp Ala Arg Phe Ala Asp Ala 2385 2390 2395 2400 Arg Leu Val Val Ile Thr Ser Gly Ala Val Ala Thr Gly Asp Asp Phe 2405 2410 2415 Leu Pro Asp Pro Ala Ala Ala Ala Val Arg Gly Leu Val Glu Gln Ala 2420 2425 2430 Gln Val Arg His Pro Gly Arg Ile Leu Leu Val Asp Thr Glu Ala Gly 2435 2440 2445 Ala Gly Leu Gly Val Gly Ala Gly Val Asp Asp Ala Leu Leu Glu Gln 2450 2455 2460 Ala Val Ala Met Ala Leu Gly Ala Asp Glu Pro Gln Leu Ala Leu Arg 2465 2470 2475 2480 Ala Gly Arg Val Leu Ala Pro Arg Leu Thr Ala Pro Gln Asp Ala Ala 2485 2490 2495 Val Thr Glu Ala Ala Arg Pro Leu Asp Pro Asp Gly Thr Val Leu Ile 2500 2505 2510 Thr Gly Pro Ala Gly Ala Pro Val Ala Asp Leu Ala Glu His Leu Val 2515 2520 2525 Arg Thr Gly Gln Cys Arg His Leu Leu Leu Leu Pro Gly Asp Gly Glu 2530 2535 2540 Leu Glu Glu Met Ala Glu Glu Leu Arg Gly Leu Gly Ala Thr Val Asp 2545 2550 2555 2560 Leu Ser Thr Ala Asp Pro Ala Asp Pro Thr Ala Leu Ala Glu Val Val 2565 2570 2575 Ala Ala Val Glu Gly Asp His Pro Leu Thr Gly Val Ile His Ala Thr 2580 2585 2590 Gly Val Val Asp Ala Phe Asp Pro Gly Asp Ser Ala Ser Asp Leu Met 2595 2600 2605 Ile Asp Ser Ala Ser Asp Ser Phe Ala Glu Ala Trp Ser Ser Arg Ala 2610 2615 2620 Gly Val Thr Ala Ala Leu His Thr Ala Thr Ala His Leu Pro Leu Asp 2625 2630 2635 2640 Leu Phe Ala Val Leu Ser Pro Ala Gly Ala Asp Leu Gly Ile Ala Arg 2645 2650 2655 Ser Ala Ala Ala Ala Gly Ala Asp Ala Phe Ser Ala Ala Leu Ala Leu 2660 2665 2670 Arg Arg His Thr Thr Val Thr Thr Asp Thr Thr Ala Pro Pro Arg Thr 2675 2680 2685 Thr Ala Pro Pro Arg Thr Thr Ala Ser Pro Arg Thr Thr Ala Leu Ser 2690 2695 2700 Ser Ser Arg Thr Thr Gly Val Ala Leu Ala Tyr Gly Pro Pro Thr Ala 2705 2710 2715 2720 Pro Arg Pro Gly Ile Lys Gly Thr Ala Pro Gly Arg Ile Pro Val Leu 2725 2730 2735 Leu Asp Ala Ala Arg Ala His Gly Gly Gly Ser Pro Leu Leu Gly Ala 2740 2745 2750 Arg Leu Ala Ala Arg Ala Leu Ala Ala Glu Ser Ala Ala Glu Gly Val 2755 2760 2765 Ala Gly Leu Pro Ala Pro Leu Arg Ala Leu Ala Val Ala Ala Ala Ala 2770 2775 2780 Ala Gly Ala Pro Thr Arg Arg Thr Ala Ala Asp Arg Lys Pro Pro Ala 2785 2790 2795 2800 Asp Trp Pro Ala Arg Leu Ala Pro Leu Ser Ala Pro Glu Gln Leu Arg 2805 2810 2815 Leu Leu Ile Asp Ala Val Arg Thr His Ala Ala Ala Val Leu Gly Arg 2820 2825 2830 Thr Asp Pro Glu Ala Leu Arg Gly Asp Ala Thr Phe Lys Gln Leu Gly 2835 2840 2845 Leu Asp Ser Leu Thr Ala Val Glu Leu Arg Asn Arg Leu Val Glu Asp 2850 2855 2860 Thr Gly Leu Arg Leu Pro Thr Ala Leu Val Phe Arg Tyr Pro Thr Pro 2865 2870 2875 2880 Ala Ala Ile Ala Ala His Leu Arg Glu Arg Leu Thr Ser Pro Ser Glu 2885 2890 2895 Thr Thr Ala Thr Gln Arg Ser Gly Gly Gln Thr Pro Ala Ala Gly Gln 2900 2905 2910 Ala Ser Ser Ala Leu Ala Pro Gly Gly Ser Ala Ala Gly Pro Pro Ala 2915 2920 2925 Ala Asp Thr Val Leu Ser Asp Leu Thr Arg Met Glu Asn Thr Leu Ser 2930 2935 2940 Val Leu Ala Ala Gln Leu Pro His Thr Glu Thr Gly Glu Ile Thr Thr 2945 2950 2955 2960 Arg Leu Glu Ala Leu Leu Thr Arg Trp Lys Thr Thr Asn Ala Thr Ala 2965 2970 2975 Asn Asp Ser Gly Asp Gly Asn Gly Gly Asp Asp Asp Ala Ala Glu Arg 2980 2985 2990 Leu Lys Ala Ala Ser Ala Asp Gln Ile Phe Asp Phe Ile Asp Asn Glu 2995 3000 3005 Leu Gly Val Gly His Gly Thr Ser Arg Val Thr Pro Thr Pro Lys Ala 3010 3015 3020 Gly 3025 20 2238 PRT Streptomyces cinnamonensis 20 Met Ala Ser Glu Glu Gln Leu Val Glu Tyr Leu Arg Arg Val Thr Thr 1 5 10 15 Glu Leu His Asp Thr Arg Arg Arg Leu Val Gln Glu Glu Asp Arg Arg 20 25 30 Gln Glu Pro Val Ala Leu Val Gly Met Ala Cys Arg Phe Pro Gly Gly 35 40 45 Val Ala Ser Pro Glu Asp Leu Trp Asp Leu Val Ala Ala Gly Lys Asp 50 55 60 Ala Ile Glu Asp Phe Pro Thr Asp Arg Gly Trp Asp Leu Glu Ala Leu 65 70 75 80 Tyr Asp Pro Asp Pro Ala Ala Tyr Gly Thr Ser Tyr Val Arg His Gly 85 90 95 Gly Phe Val Asp Asp Ala Gly Ser Phe Asp Ala Asp Phe Phe Gly Ile 100 105 110 Ser Pro Arg Glu Ala Leu Ala Met Asp Pro Gln Gln Arg Leu Met Leu 115 120 125 Glu Thr Ser Trp Glu Leu Phe Glu Arg Ala Gly Ile Glu Pro Val Ser 130 135 140 Leu Lys Gly Ser Arg Thr Gly Val Tyr Ala Gly Val Ser Ser Glu Asp 145 150 155 160 Tyr Met Ser Gln Leu Pro Arg Ile Pro Glu Gly Phe Glu Gly His Ala 165 170 175 Thr Thr Gly Ser Leu Thr Ser Val Ile Ser Gly Arg Val Ala Tyr Asn 180 185 190 Tyr Gly Leu Glu Gly Pro Ala Val Thr Val Asp Thr Ala Cys Ser Ala 195 200 205 Ser Leu Val Ala Ile His Leu Ala Ser Gln Ala Leu Arg Gln Arg Glu 210 215 220 Cys Asp Leu Ala Leu Ala Gly Gly Val Leu Val Leu Ser Ser Pro Leu 225 230 235 240 Met Phe Thr Glu Phe Cys Arg Gln Arg Gly Leu Ala Pro Asp Gly Arg 245 250 255 Cys Lys Pro Phe Ala Ala Ala Ala Asp Gly Thr Gly Phe Ser Glu Gly 260 265 270 Ile Gly Leu Leu Leu Leu Glu Arg Leu Ser Asp Ala Arg Arg Asn Gly 275 280 285 His Lys Val Leu Ala Val Ile Arg Gly Ser Ala Val Asn Gln Asp Gly 290 295 300 Ala Ser Asn Gly Leu Thr Ala Pro Asn Asp Ala Ala Gln Glu Gln Val 305 310 315 320 Ile Arg Ala Ala Leu Asp Asn Ala Arg Leu Thr Pro Ser Glu Val Asp 325 330 335 Ala Val Glu Ala His Gly Thr Gly Thr Lys Leu Gly Asp Pro Ile Glu 340 345 350 Ala Gly Ala Leu Leu Ala Thr Tyr Gly Gln His Arg Ala Arg Pro Leu 355 360 365 Leu Leu Gly Ser Leu Lys Ser Asn Ile Gly His Thr His Ala Thr Ala 370 375 380 Gly Val Ala Gly Val Ile Lys Thr Val Met Ala Ile Arg Asn Gly Leu 385 390 395 400 Leu Pro Ala Thr Leu His Val Glu Glu Leu Ser Pro His Val Asp Trp 405 410 415 Asp Ala Gly Ala Val Glu Val Val Thr Glu Pro Thr Pro Trp Pro Glu 420 425 430 Thr Gly His Pro Arg Arg Ala Gly Val Ser Ala Phe Gly Ile Ser Gly 435 440 445 Thr Asn Ala His Leu Ile Leu Glu Glu Ala Pro Pro Glu Glu Asp Val 450 455 460 Pro Ala Pro Val Val Val Glu Ser Gly Gly Val Val Pro Trp Val Val 465 470 475 480 Ser Gly Arg Thr Pro Glu Ala Leu Arg Glu Gln Ala Arg Arg Leu Gly 485 490 495 Glu Phe Val Ala Gly Asp Thr Asp Ala Leu Pro Asn Glu Val Gly Trp 500 505 510 Ser Leu Ala Thr Thr Arg Ser Val Phe Glu His Arg Ala Val Val Val 515 520 525 Gly Arg Asp Arg Asp Ala Leu Thr Ala Gly Leu Gly Ala Leu Ala Ala 530 535 540 Gly Glu Ala Ser Ala Gly Val Val Ala Gly Val Ala Gly Asp Val Gly 545 550 555 560 Pro Gly Pro Val Leu Val Phe Pro Gly Gln Gly Ala Gln Trp Val Gly 565 570 575 Met Gly Ala Gln Leu Leu Asp Glu Ser Ala Val Phe Ala Ala Arg Ile 580 585 590 Ala Glu Cys Glu Arg Ala Leu Ser Ala His Val Asp Trp Ser Leu Ser 595 600 605 Ala Val Leu Arg Gly Asp Gly Ser Glu Leu Ser Arg Val Glu Val Val 610 615 620 Gln Pro Val Leu Trp Ala Val Met Val Ser Leu Ala Ala Val Trp Ala 625 630 635 640 Asp Tyr Gly Val Thr Pro Ala Ala Val Ile Gly His Ser Gln Gly Glu 645 650 655 Met Ala Ala Ala Cys Val Ala Gly Ala Leu Ser Leu Glu Asp Ala Ala 660 665 670 Arg Ile Val Ala Val Arg Ser Asp Ala Leu Arg Gln Leu Gln Gly His 675 680 685 Gly Asp Met Ala Ser Leu Ser Thr Gly Ala Glu Gln Ala Ala Glu Leu 690 695 700 Ile Gly Asp Arg Pro Gly Val Val Val Ala Ala Val Asn Gly Pro Ser 705 710 715 720 Ser Thr Val Ile Ser Gly Pro Pro Glu His Val Ala Ala Val Val Ala 725 730 735 Asp Ala Glu Ala Arg Gly Leu Arg Ala Arg Val Ile Asp Val Gly Tyr 740 745 750 Ala Ser His Gly Pro Gln Ile Asp Gln Leu His Asp Leu Leu Thr Glu 755 760 765 Arg Leu Ala Asp Ile Arg Pro Thr Asn Thr Asp Val Ala Phe Tyr Ser 770 775 780 Thr Val Thr Ala Glu Arg Leu Thr Asp Thr Thr Ala Leu Asp Thr Asp 785 790 795 800 Tyr Trp Val Thr Asn Leu Arg Gln Pro Val Arg Phe Ala Asp Thr Ile 805 810 815 Glu Ala Leu Leu Ala Asp Gly Tyr Arg Leu Phe Ile Glu Ala Ser Ala 820 825 830 His Pro Val Leu Gly Leu Gly Met Glu Glu Thr Ile Glu Gln Ala Asp 835 840 845 Met Pro Ala Thr Val Val Pro Thr Leu Arg Arg Asp His Gly Asp Thr 850 855 860 Thr Gln Leu Thr Arg Ala Ala Ala His Ala Phe Thr Ala Gly Ala Asp 865 870 875 880 Val Asp Trp Arg Arg Trp Phe Pro Ala Asp Pro Ala Pro Arg Thr Ile 885 890 895 Asp Leu Pro Thr Tyr Ala Phe Gln Arg Arg Arg Tyr Trp Leu Ala Asp 900 905 910 Thr Val Lys Arg Asp Ser Gly Trp Asp Pro Ala Gly Ser Gly His Ala 915 920 925 Gln Leu Pro Thr Ala Val Ala Leu Ala Asp Gly Gly Val Val Leu Asn 930 935 940 Gly Arg Val Ser Ala Glu Arg Gly Gly Trp Leu Gly Gly His Val Val 945 950 955 960 Ala Gly Thr Val Leu Val Pro Gly Ala Ala Leu Val Glu Trp Val Leu 965 970 975 Arg Ala Gly Asp Glu Ala Gly Cys Pro Ser Leu Glu Glu Leu Thr Leu 980 985 990 Gln Ala Pro Leu Val Leu Pro Glu Ser Gly Gly Leu Gln Val Gln Val 995 1000 1005 Val Val Gly Ala Ala Asp Glu Gln Gly Gly Arg Arg Asp Val His Val 1010 1015 1020 Tyr Ser Arg Ser Glu Gln Asp Ala Ser Ala Val Trp Gln Cys His Ala 1025 1030 1035 1040 Val Gly Glu Leu Gly Arg Ala Ser Val Ala Arg Pro Val Arg Gln Ala 1045 1050 1055 Gly Gln Trp Pro Pro Ala Gly Ala Glu Pro Val Glu Val Gly Gly Phe 1060 1065 1070 Tyr Glu Gly Val Ala Ala Ala Gly Tyr Glu Tyr Gly Pro Ala Phe Arg 1075 1080 1085 Gly Leu Arg Ala Met Trp Arg His Gly Asp Asp Leu Leu Ala Glu Val 1090 1095 1100 Glu Leu Pro Glu Glu Ala Gly Ser Pro Ala Gly Phe Gly Ile His Pro 1105 1110 1115 1120 Ala Leu Leu Asp Ala Ala Leu His Pro Leu Leu Ala Gln Arg Ser Arg 1125 1130 1135 Asp Gly Ala Gly Ala Gly Ala His Gly Gly Gln Val Leu Leu Pro Phe 1140 1145 1150 Ser Trp Ser Gly Val Ser Leu Trp Ala Ser Glu Ala Thr Thr Val Arg 1155 1160 1165 Val Arg Leu Thr Gly Leu Gly Gly Gly Asp Asp Glu Thr Val Ser Leu 1170 1175 1180 Thr Val Thr Asp Pro Ala Gly Gly Pro Val Val Asp Val Ala Glu Leu 1185 1190 1195 1200 Arg Leu Arg Ser Thr Ser Ala Arg Gln Val Arg Gly Ser Ala Gly Pro 1205 1210 1215 Gly Ala Asp Gly Leu Tyr Glu Leu Arg Trp Thr Pro Leu Pro Glu Pro 1220 1225 1230 Leu Pro Val Pro Ala Pro Ala Asn Gly Arg Asp Val Ala Ala Asp Leu 1235 1240 1245 Ser Gly Cys Ala Val Leu Gly Glu Leu Val Ala Glu Pro Gly Pro Gly 1250 1255 1260 Ile Asp Leu Glu Gly Cys Pro Cys Tyr Pro Gly Val Gly Ala Leu Ala 1265 1270 1275 1280 Asp Asn Ala Ser Pro Pro Ser Met Ile Leu Ala Pro Val His Ser Asp 1285 1290 1295 Thr Thr Gly Gly Asp Gly Leu Ala Leu Thr Glu Arg Val Leu Arg Val 1300 1305 1310 Ile Gln Asp Phe Leu Ala Ala Pro Ser Leu Glu Gln Lys Gln Thr Arg 1315 1320 1325 Leu Ala Phe Val Thr Arg Gly Ala Ala Asp Thr Gly Ser Thr Thr Gly 1330 1335 1340 Gly Ser Ala Ala Pro Ala Glu Ala Val Asp Pro Ala Val Ala Ala Val 1345 1350 1355 1360 Trp Gly Leu Val Arg Ser Ala Gln Ser Glu Asn Pro Gly Arg Phe Val 1365 1370 1375 Leu Leu Asp Thr Asp Ala Pro Leu Asp Gln Ala Ser Val Ala Pro Leu 1380 1385 1390 Val Asp Ala Val Arg Ser Ala Val Glu Ala Asp Glu Pro Gln Val Ala 1395 1400 1405 Leu Arg Gly Gly Arg Leu Leu Val Pro Arg Trp Ala Arg Ala Gly Glu 1410 1415 1420 Pro Val Glu Leu Ala Gly Pro Ala Gly Ala Arg Ala Trp Arg Leu Val 1425 1430 1435 1440 Gly Gly Asp Ser Gly Thr Leu Glu Ala Val Val Ala Glu Ala Cys Asp 1445 1450 1455 Asp Ile Val Leu Arg Pro Leu Ala Pro Gly Gln Val Arg Val Ala Val 1460 1465 1470 His Thr Ala Gly Val Asn Phe Arg Asp Val Leu Ile Ala Leu Gly Met 1475 1480 1485 Tyr Pro Asp Pro Asp Ala Leu Pro Gly Thr Glu Ala Ala Gly Val Val 1490 1495 1500 Thr Glu Val Gly Pro Gly Val Thr Arg Leu Ser Val Gly Asp Arg Val 1505 1510 1515 1520 Met Gly Met Met Asp Gly Ala Phe Gly Pro Trp Ala Val Ala Asp Ala 1525 1530 1535 Arg Met Leu Ala Pro Val Pro Pro Gly Trp Gly Thr Arg Gln Ala Ala 1540 1545 1550 Ala Ala Pro Ala Ala Phe Leu Thr Ala Trp Tyr Gly Leu Val Glu Leu 1555 1560 1565 Ala Gly Leu Lys Ala Gly Glu Arg Val Leu Ile His Ala Ala Thr Gly 1570 1575 1580 Gly Val Gly Met Ala Ala Val Gln Ile Ala Arg His Val Gly Ala Glu 1585 1590 1595 1600 Val Phe Ala Thr Ala Ser Pro Gly Lys His Ala Val Leu Glu Glu Met 1605 1610 1615 Gly Ile Asp Ala Ala His Arg Ala Ser Ser Arg Asp Leu Ala Phe Glu 1620 1625 1630 Asp Ala Phe Arg Gln Ala Thr Asp Gly Arg Gly Val Asp Val Val Leu 1635 1640 1645 Asn Ser Leu Thr Gly Glu Leu Leu Asp Ala Ser Leu Arg Leu Leu Gly 1650 1655 1660 Asp Gly Gly Arg Phe Val Glu Met Gly Lys Ser Asp Pro Arg Asp Pro 1665 1670 1675 1680 Glu Leu Val Ala Leu Glu His Pro Gly Val Ser Tyr Glu Ala Phe Asp 1685 1690 1695 Leu Val Ala Asp Ala Gly Pro Glu Arg Leu Gly Leu Met Leu Asp Arg 1700 1705 1710 Leu Gly Glu Leu Phe Ala Gly Gly Ser Leu Val Pro Leu Pro Val Thr 1715 1720 1725 Ala Trp Pro Leu Gly Arg Ala Arg Glu Ala Leu Arg His Met Ser Gln 1730 1735 1740 Ala Arg His Thr Gly Lys Leu Val Leu Asp Val Pro Ala Pro Leu Asp 1745 1750 1755 1760 Pro Asp Gly Thr Val Leu Val Thr Gly Gly Thr Gly Thr Ile Gly Ala 1765 1770 1775 Ala Val Ala Glu His Leu Ala Arg Thr Gly Glu Ser Lys His Leu Leu 1780 1785 1790 Ile Val Ser Arg Ser Gly Pro Ala Ala His Gly Ala Glu Glu Leu Val 1795 1800 1805 Ser Arg Ile Ala Glu Phe Gly Ala Glu Ala Thr Phe Val Ala Ala Asp 1810 1815 1820 Val Ser Glu Pro Asp Ala Val Ala Ala Leu Ile Glu Gly Ile Asp Pro 1825 1830 1835 1840 Ala His Pro Leu Thr Gly Val Val His Ala Ala Gly Val Leu Asp Asn 1845 1850 1855 Ala Leu Ile Gly Ser Gln Thr Thr Glu Ser Leu Thr Arg Val Trp Ala 1860 1865 1870 Ala Lys Ala Ala Ala Ala Gln Gln Leu His Glu Ala Thr Arg Glu Ser 1875 1880 1885 Arg Leu Gly Leu Phe Val Met Phe Ser Ser Phe Ala Ser Thr Met Gly 1890 1895 1900 Thr Pro Gly Gln Ala Asn Tyr Ser Ala Ala Asn Ala Tyr Cys Asp Ala 1905 1910 1915 1920 Leu Ala Ala Leu Arg Arg Ala Glu Gly Leu Ala Gly Leu Ser Val Ala 1925 1930 1935 Trp Gly Leu Trp Glu Ala Thr Ser Gly Leu Thr Gly Thr Leu Ser Ala 1940 1945 1950 Ala Asp Arg Ala Arg Ile Asp Arg Tyr Gly Ile Arg Pro Thr Ser Ala 1955 1960 1965 Ala Arg Gly Cys Ala Leu Leu Ala Ala Ala Arg Ala His Gly Arg Pro 1970 1975 1980 Asp Leu Leu Ala Met Asp Leu Asp Ala Arg Val Pro Ala Ala Ser Asp 1985 1990 1995 2000 Ala Pro Val Pro Ala Val Leu Arg Thr Leu Ala Ala Ala Gly Ala Pro 2005 2010 2015 Ala Thr Ala Arg Pro Thr Ala Ala Ala Ala Ala Asp Gly Ala Thr Asp 2020 2025 2030 Trp Ser Gly Arg Leu Ala Gly Leu Thr Glu Glu Ala Arg Leu Glu Leu 2035 2040 2045 Leu Thr Glu Leu Val Cys Thr His Ala Ala Gly Val Leu Gly His Ala 2050 2055 2060 Asp Ala Gly Ala Val Gln Val Asp Ala Pro Phe Lys Glu Leu Gly Phe 2065 2070 2075 2080 Asp Ser Leu Thr Ala Val Glu Leu Arg Asn Arg Ile Ala Ala Ala Thr 2085 2090 2095 Gly Leu Lys Leu Pro Ala Ala Leu Val Phe Asp Tyr Pro Gln Ala Arg 2100 2105 2110 Val Leu Ala Ala His Leu Ala Glu Arg Leu Val Pro Glu Gly Ala Gly 2115 2120 2125 Ala Met Gly Gly Val Ser Gly Ala Glu Gly Val Arg Asp Ala Tyr Gly 2130 2135 2140 Ala Gly Gly Pro Gly Gly Asp Met Thr Ala Gln Val Leu Leu Glu Val 2145 2150 2155 2160 Ala Arg Val Glu His Thr Leu Ser Ala Ala Val Pro His Gly Leu Asp 2165 2170 2175 Arg Ala Ala Val Ala Ala Arg Leu Glu Ala Leu Leu Ala Arg Cys Thr 2180 2185 2190 Ala Thr Thr Ala Ala Thr Gly Ala Ala Gly Ala Ala Val Glu Gly Asp 2195 2200 2205 Gly Asp Ser Asp Gly Asp Gly Ala Val Asp Gln Leu Glu Thr Ala Thr 2210 2215 2220 Ala Glu Gln Val Leu Asp Phe Ile Asp Asn Glu Leu Gly Val 2225 2230 2235 21 4132 PRT Streptomyces cinnamonensis 21 Met Val Ser Glu Glu Lys Leu Val Asp Tyr Leu Lys Arg Val Ser Ala 1 5 10 15 Asp Leu His Ala Thr Arg Gln Arg Leu Arg Glu Ala Glu Glu Arg Gly 20 25 30 Gln Glu Pro Val Ala Val Val Glu Ala Ala Cys Arg Tyr Pro Gly Gly 35 40 45 Ile Arg Thr Pro Glu Asp Leu Trp Asp Leu Val Ala Ala Gly Gly Asn 50 55 60 Ala Leu Gly Ala Phe Pro Asp Asn Arg Gly Trp Asp Leu Arg Arg Leu 65 70 75 80 Phe His Pro Asp Pro Asp His Pro Gly Thr Thr Tyr Ala Arg Glu Gly 85 90 95 Gly Phe Leu His Asp Ala Asp Leu Phe Asp Pro Glu Phe Phe Gly Ile 100 105 110 Ser Pro Arg Glu Ala Ala Val Leu Asp Pro Gln Gln Arg Leu Leu Leu 115 120 125 Glu Cys Ala Trp Glu Ala Leu Glu Arg Ala Gly Ile Asp Pro Arg Ser 130 135 140 Leu Gln Gly Ser Arg Thr Gly Val Tyr Ala Gly Ala Ala Leu Pro Gly 145 150 155 160 Phe Gly Thr Pro His Ile Asp Pro Ala Ala Glu Gly His Leu Val Thr 165 170 175 Gly Ser Ala Pro Ser Val Leu Ser Gly Arg Leu Ala Tyr Thr Phe Gly 180 185 190 Leu Glu Gly Pro Ala Val Thr Ile Asp Thr Ala Cys Ser Ser Ser Leu 195 200 205 Val Ala Val His Leu Ala Ala His Ala Leu Arg Gln Arg Glu Cys Asp 210 215 220 Leu Ala Leu Ala Gly Gly Val Thr Val Met Thr Thr Pro Tyr Val Phe 225 230 235 240 Thr Glu Phe Ser Arg Gln Arg Gly Leu Ala Ala Asp Gly Arg Cys Lys 245 250 255 Pro Phe Ala Ala Ala Ala Asp Gly Thr Ala Phe Ser Glu Gly Ala Gly 260 265 270 Leu Leu Val Leu Glu Arg Leu Ser Asp Ala Arg Arg Ala Gly His Arg 275 280 285 Val Leu Ala Val Ile Arg Gly Ser Ala Val Asn Gln Asp Gly Ala Ser 290 295 300 Asn Gly Leu Thr Ala Pro Asn Gly Pro Ala Gln Gln Arg Val Ile Arg 305 310 315 320 Ala Ala Leu Ala Gly Ala Arg Leu Ser Pro Ala Glu Val Asp Ala Val 325 330 335 Glu Ala His Gly Thr Gly Thr Arg Leu Gly Asp Pro Ile Glu Ala Asp 340 345 350 Ala Leu Leu Ala Thr Tyr Gly Gln Glu Arg His Gly Gly Arg Pro Leu 355 360 365 Trp Leu Gly Ser Val Lys Ser Asn Ile Gly His Thr Gln Gly Ala Ala 370 375 380 Gly Ala Ala Gly Leu Ile Lys Met Val Gln Ala Leu Arg His Glu Thr 385 390 395 400 Leu Pro Ala Thr Leu Tyr Ala Asp Glu Pro Thr Pro His Ala Asp Trp 405 410 415 Glu Ser Gly Ala Val Arg Leu Leu Ser Ala Pro Val Ala Trp Pro Arg 420 425 430 Gly Glu His Gly Glu His Thr Arg Arg Ala Gly Ile Ser Ser Phe Gly 435 440 445 Ile Ser Gly Thr Asn Ala His Leu Ile Leu Glu Glu Ala Pro Ala Ala 450 455 460 Asp Ala Glu Gly Ala Gly Gly Asp Gly Asp Gly Asp Gly Gly Gly Val 465 470 475 480 Arg Pro Val Val Arg Val Gly Ala Thr Gly Pro Arg Glu Glu Gln Gly 485 490 495 Gln Gly Gln Gly Gln Glu Gln His Gln Gln Gln Arg Gln Gln Arg Gln 500 505 510 Arg Ser Ser Met Met Pro Thr Pro His Leu Pro Trp Leu Leu Ser Ala 515 520 525 Arg Ser Pro Ala Ala Leu Arg Ala Gln Ala Asp Ala Leu Ala Asn His 530 535 540 Val Ala His Ala Asp His Ser Ile Ala Asp Ile Gly Gly Thr Leu Leu 545 550 555 560 Arg Arg Thr Leu Phe Glu His Arg Ala Val Val Leu Gly Thr Asp Arg 565 570 575 Asp Glu Arg Ala Ala Ala Leu Ala Ala Leu Ala Ala Gly Arg Ala His 580 585 590 Pro Ala Leu Thr Arg Ala Ala Gly Pro Ala Arg Asn Gly Gly Thr Ala 595 600 605 Phe Leu Phe Thr Gly Gln Gly Ser Gln Arg Pro Gly Met Gly Arg Gln 610 615 620 Leu Tyr Asp Thr Phe Asp Val Phe Ala Glu Ser Leu Asp Glu Thr Cys 625 630 635 640 Ala Arg Leu Asp Pro Leu Leu Glu Gln Pro Leu Lys Pro Val Leu Phe 645 650 655 Ala Pro Ala Asp Thr Ala Gln Ala Ala Val Leu His Gly Thr Gly Met 660 665 670 Thr Gln Ala Ala Leu Phe Ala Leu Glu Val Ala Leu Tyr Arg Gln Val 675 680 685 Thr Ser Phe Gly Ile Ala Pro Ser His Leu Thr Gly His Ser Val Gly 690 695 700 Glu Ile Ala Ala Ala His Val Ala Gly Val Phe Ser Leu Ala Asp Ala 705 710 715 720 Cys Thr Leu Val Ala Ala Arg Gly Arg Leu Met Gln Ala Leu Pro Ala 725 730 735 Gly Gly Ala Met Leu Ala Val Gln Ala Ala Glu Asp Asp Val Leu Pro 740 745 750 Leu Leu Ala Gly Gln Glu Glu Arg Leu Ser Leu Ala Ala Val Asn Gly 755 760 765 Pro Thr Ala Val Val Val Ser Gly Glu Ala Ala Ala Val Gly Glu Val 770 775 780 Glu Lys Ala Leu Arg Gly Arg Gly Leu Lys Thr Lys Arg Leu Asn Val 785 790 795 800 Ser His Ala Phe His Ser Pro Leu Ile Glu Pro Met Leu Asp Asp Phe 805 810 815 Arg Glu Val Ala Arg Gly Leu Thr Phe His Ala Pro Thr Leu Pro Val 820 825 830 Val Ser Asn Leu Thr Gly Arg Leu Ala Asp Ala Glu Leu Met Ala Asp 835 840 845 Ala Glu Tyr Trp Val Arg His Val Arg Arg Pro Val Arg Phe His Asp 850 855 860 Gly Leu Arg Ala Leu Ser Glu Gln Gly Val Val Arg Tyr Leu Glu Leu 865 870 875 880 Gly Pro Asp Pro Val Leu Ala Thr Met Val Gln Asp Gly Leu Pro Ala 885 890 895 Pro Ala Glu Gly Glu Glu Pro Glu Pro Val Val Ala Ala Ala Leu Arg 900 905 910 Ser Lys His Asp Glu Gly Arg Thr Leu Leu Gly Ala Val Ala Ala Leu 915 920 925 His Thr Asp Gly Gln Pro Ala Asp Leu Thr Ala Leu Phe Pro Ala Asp 930 935 940 Ala Gly Gln Val Pro Leu Pro Thr Tyr Arg Phe Gln Arg Arg Arg Tyr 945 950 955 960 Trp Arg Val Ala Pro Asp Ala Ala Ala Pro Ala Arg Ala Ala Gly Leu 965 970 975 Gln Glu Thr Gly His Pro Leu Leu Pro Ala Val Ile Arg Gln Ala Asp 980 985 990 Gly Gly Ile Leu Leu Ala Gly Arg Leu Ser Leu Arg Thr His Pro Trp 995 1000 1005 Leu Ala Asp His Thr Ile Ala Gly Gly Val Pro Leu Pro Ala Thr Ala 1010 1015 1020 Phe Val Glu Leu Ala Leu Leu Ala Gly Arg His Ala Ala Cys Asp Thr 1025 1030 1035 1040 Ile Asp Asp Leu Thr Leu Glu Thr Pro Leu Leu Leu Asp Asp Thr Gly 1045 1050 1055 Thr Gly Val Gly Ala Ala Val Gly Ala Gly Ala Asp Ala Leu Val Asp 1060 1065 1070 Ala Ile Glu Val Gln Leu Ala Leu Gly Ala Pro Asp Gly Ser Gly Arg 1075 1080 1085 Arg Ala Leu Thr Val His Ser Arg Pro Ala Asp Asp Ala Ala Asp Asp 1090 1095 1100 Gly Asp Ala Ala Asp Ala Ala Asp Ala Ala Gly Arg Gly Gly Pro Gly 1105 1110 1115 1120 Gly Ser Gly Asp Leu Gly Asp Pro Gly Asp Pro Gly Asp Leu Gly Asp 1125 1130 1135 Gly Gly Gly Ser Arg Gly Trp Arg Arg His Ala Thr Gly Ile Leu Ser 1140 1145 1150 Ala Gly Pro Ala Ala Glu Pro Ala Ala Pro Asp Ala Ala Pro Trp Pro 1155 1160 1165 Pro Ala Asp Ala Thr Ala Leu Asp Val Asp Ala Leu Tyr Ala Arg Leu 1170 1175 1180 Asp Ala Gln Gly Tyr Ser Tyr Gly Pro Ala Phe Arg Ala Val His Ala 1185 1190 1195 1200 Ala Trp Arg His Gly Asp Asp Leu Tyr Ala Asp Val Arg Leu Ala Asp 1205 1210 1215 Glu Gln Arg Ala Glu Ala Asp Ala Phe Ala Leu His Pro Ala Leu Leu 1220 1225 1230 Asp Ala Ala Leu His Ala Val Asp Glu Leu Tyr Arg Gly Ser Glu Gly 1235 1240 1245 Arg Gly Gln Glu Gln Gly Gln Gly Gly Gln Glu Pro Glu Gln Gly Arg 1250 1255 1260 Gly Asp Ala Asp Ala Pro Val Arg Leu Pro Phe Ser Phe Ser Asp Ile 1265 1270 1275 1280 Arg His His Ala Thr Gly Ala Thr Arg Leu Trp Val Arg Leu Ser Pro 1285 1290 1295 Gln Gly Asp Asp Arg Leu Arg Leu Ser Leu Thr Asp Gly Glu Gly Gly 1300 1305 1310 Gln Val Ala Thr Val Asp Ala Leu Gln Leu Arg Leu Ile Pro Ala Asp 1315 1320 1325 Arg Trp Arg Ala Ala Arg Pro Thr Thr Ala Ala Pro Leu Tyr His Leu 1330 1335 1340 Asp Trp His Glu Leu Pro Leu Pro Glu Pro Ala Glu Thr Asp Pro Ala 1345 1350 1355 1360 Ala His Ser Trp Ala Val Leu Gly Ala His Asp Ala Gly Leu Ala Pro 1365 1370 1375 Ala Ala His Tyr Pro Asp Leu Ala Ala Leu Lys Ala Ala Val Glu Ala 1380 1385 1390 Gly Glu Pro Val Pro Asp Ile Val Phe Ala Pro Phe Pro Ala Gln Gly 1395 1400 1405 Thr Glu Thr Asp Val Pro Ala Gln Val Arg Ala His Ala Arg His Ala 1410 1415 1420 Leu Glu Leu Leu Arg Asp Trp Leu Thr Thr Glu Ala Phe Ala Ala Ala 1425 1430 1435 1440 Arg Leu Val Val Leu Thr Thr Gly Ala Val Thr Ala Arg Pro Glu Asp 1445 1450 1455 Gly Pro Ala Asp Leu Ala Thr Ala Pro Val Trp Gly Leu Val Arg Ala 1460 1465 1470 Ala Gln Ala Glu Gln Pro Asp His Val Val Leu Val Asp Ile Asp Lys 1475 1480 1485 Asp Ile Asp Lys Asp Thr Asp Glu Glu Thr Asp Gln Ala Thr Asp Ala 1490 1495 1500 Gly Thr Ala Ser Arg His Ala Leu Pro Ala Ala Leu Ala Ala Ala Ala 1505 1510 1515 1520 Ala Gln Ala Glu Thr Gln Leu Ala Leu Arg Ala Gly Thr Val Leu Val 1525 1530 1535 Pro Arg Leu Ala Val Val Pro Pro Arg Thr Asp Thr Pro Ala Leu His 1540 1545 1550 Ala Thr Ala Pro Glu Ser Thr Thr Asp Thr Val Asp Ser Thr Gly Ile 1555 1560 1565 Ala Gly Ala Ala Glu Ser Gly Gly Thr Val Leu Ile Thr Gly Gly Thr 1570 1575 1580 Gly Gly Leu Gly Gln Ala Val Ala Arg His Leu Ala Ala Ala His Gly 1585 1590 1595 1600 Ala Arg His Leu Leu Leu Val Ser Arg Arg Gly Asp Ala Ala Glu Gly 1605 1610 1615 Val Ala Glu Leu Arg Ala Asp Leu Ala Asp Asp Gly Val Asp Val Arg 1620 1625 1630 Val Ala Ala Cys Asp Ile Thr Asp Arg Asp Ala Leu Ala Gly Leu Leu 1635 1640 1645 Ala Asp Ile Pro Ala Ala His Pro Leu Thr Ala Val Val His Thr Ala 1650 1655 1660 Gly Val Ile Asp Asp Ser Leu Ile Thr Ala Met Thr Pro Glu Arg Leu 1665 1670 1675 1680 Asp Ala Val Leu Ala Pro Lys Ala Asp Ala Ala Trp His Leu His Glu 1685 1690 1695 Leu Thr Arg Asp Lys Asp Leu Ser Ala Phe Val Leu Phe Ser Ser Gly 1700 1705 1710 Ala Ser Val Leu Gly Asn Gly Gly Gln Ala Asn Tyr Ala Ala Ala Asn 1715 1720 1725 Thr Phe Leu Asn Thr Leu Ala Glu His Arg Arg Ala Ala Gly Leu Ala 1730 1735 1740 Ala Thr Ser Val Ala Trp Gly Leu Trp Glu Ser Ala Ser Gly Gly Met 1745 1750 1755 1760 Ala Ala Arg Leu Gly Asp Ala Asp Arg Ala Arg Ile His Arg Thr Gly 1765 1770 1775 Val Thr Gly Leu Thr Asp Glu Gln Ala Leu Ala Leu Phe Asp Ala Ala 1780 1785 1790 Leu Thr Ala Glu His Pro Thr Val Leu Ala Thr Arg Phe Asp Arg Ala 1795 1800 1805 Val Leu Arg Gly Gln Ala Ala Ala Arg Thr Leu Gln Pro Ala Leu Arg 1810 1815 1820 Gly Leu Val Arg Thr Pro Arg Pro Thr Ala Ser Ala Gly Ala Ile Gly 1825 1830 1835 1840 Ser Thr Ala Ala Thr Gly Ser Ala Thr Asp Glu Asn Ala Pro Ser Ser 1845 1850 1855 Trp Ala Ala Arg Leu Ala Arg Leu Ser Ala Ala Asp Arg Asp Arg Ala 1860 1865 1870 Leu Asn Glu Leu Ile Arg Glu Gln Ile Ala Thr Val Leu Ala His Pro 1875 1880 1885 Ser Pro Asp Thr Ile Glu Leu Gly Arg Ala Phe Gln Glu Leu Gly Phe 1890 1895 1900 Asp Ser Leu Thr Ala Leu Glu Leu Arg Asn Arg Leu Ser Thr Ala Thr 1905 1910 1915 1920 Gly Ile Arg Leu Pro Ala Thr Leu Val Phe Asp His Pro Ser Pro Thr 1925 1930 1935 Ala Leu Val Arg His Leu His Ser His Leu Pro Asp Glu Ala Gln His 1940 1945 1950 Thr Ser Pro Thr Ala Pro Gly Ala Ser Ala Glu Gly Thr Ala Ala Thr 1955 1960 1965 Ala Thr Gly Ile Asp Asp Asp Pro Ile Ala Ile Val Gly Met Ala Cys 1970 1975 1980 Arg Tyr Pro Gly Gly Val Thr Ser Pro Glu Gln Leu Trp Gln Leu Val 1985 1990 1995 2000 Ala Thr Gly Thr Asp Ala Ile Gly Pro Phe Pro Glu Asp Arg Gly Trp 2005 2010 2015 Asp Thr Ala Gly Leu Phe Asp Pro Asp Pro Asp Gln Val Gly His Ser 2020 2025 2030 Tyr Thr Arg Glu Gly Gly Phe Leu Tyr Asp Ala Ala Arg Phe Asp Ala 2035 2040 2045 Gly Phe Phe Gly Ile Ser Pro Arg Glu Ala Ala Ala Thr Asp Pro Gln 2050 2055 2060 Gln Arg Leu Leu Leu Glu Thr Ala Trp Gln Ala Phe Glu His Ala Gly 2065 2070 2075 2080 Ile Asp Pro Ala Ala Leu Arg Gly Thr Pro Cys Gly Val Ile Thr Gly 2085 2090 2095 Ile Met Tyr Asp Asp Tyr Gly Ser Arg Phe Leu Ala Arg Lys Pro Asp 2100 2105 2110 Gly Phe Glu Gly Arg Ile Met Thr Gly Ser Thr Pro Ser Val Ala Ser 2115 2120 2125 Gly Arg Val Ala Tyr Thr Phe Gly Leu Glu Gly Pro Ala Ile Thr Val 2130 2135 2140 Asp Thr Ala Cys Ser Ser Ser Leu Val Ala Met His Leu Ala Ala Gln 2145 2150 2155 2160 Ala Leu Arg Gln Gly Glu Cys Glu Leu Ala Leu Ala Gly Gly Val Thr 2165 2170 2175 Val Met Ala Thr Pro Asn Thr Phe Val Glu Phe Ser Arg Gln Arg Gly 2180 2185 2190 Leu Ala Pro Asp Gly Arg Cys Lys Pro Phe Ala Ala Ala Ala Asp Gly 2195 2200 2205 Thr Gly Trp Gly Glu Gly Ala Gly Leu Val Val Leu Glu Arg Leu Ser 2210 2215 2220 Asp Ala Arg Arg Lys Gly His Arg Val Leu Ala Leu Leu Arg Gly Ser 2225 2230 2235 2240 Ala Val Asn Gln Asp Gly Ala Ser Asn Gly Met Thr Ala Pro Asn Gly 2245 2250 2255 Pro Ser Gln Glu Arg Val Ile Arg Thr Ala Leu Ala Gly Ala Gly Arg 2260 2265 2270 Gly Pro Glu Asp Ile Asp Val Val Glu Ala His Gly Thr Gly Thr Thr 2275 2280 2285 Leu Gly Asp Pro Ile Glu Ala Gln Ala Leu Leu Ala Thr Tyr Gly Gln 2290 2295 2300 Gly Arg Pro Glu Asp Arg Pro Leu Trp Leu Gly Ser Val Lys Ser Asn 2305 2310 2315 2320 Ile Gly His Thr Gln Ala Ala Ala Gly Val Ala Gly Val Ile Lys Met 2325 2330 2335 Val Met Ala Leu Arg His Glu Gln Leu Pro Thr Thr Leu His Ala Asp 2340 2345 2350 Glu Pro Thr Pro His Val Gln Trp Asp Gly Gly Gly Val Arg Leu Leu 2355 2360 2365 Thr Glu Pro Val Pro Trp Ser Arg Gly Glu Arg Thr Arg Arg Ala Gly 2370 2375 2380 Val Ser Ser Phe Gly Ile Ser Gly Thr Asn Ala His Leu Ile Leu Glu 2385 2390 2395 2400 Glu Pro Pro Glu Glu Asp Leu Pro Glu Pro Val Ala Ala Glu Pro Gly 2405 2410 2415 Gly Val Val Pro Trp Val Val Ser Gly Arg Thr Pro Asp Ala Leu Arg 2420 2425 2430 Glu Gln Ala Arg Arg Leu Gly Glu Phe Val Val Gly Ala Gly Asp Val 2435 2440 2445 Ser Ala Ala Glu Val Gly Trp Ser Leu Ala Thr Thr Arg Ser Val Phe 2450 2455 2460 Glu His Arg Ala Val Val Ala Gly Arg Asp Arg Asp Asp Leu Val Ala 2465 2470 2475 2480 Gly Met Gln Ala Leu Ala Ala Gly Glu Thr Pro Thr Asp Val Val Ser 2485 2490 2495 Gly Ala Ala Ala Ser Ser Gly Ala Gly Pro Val Leu Val Phe Pro Gly 2500 2505 2510 Gln Gly Ser Gln Trp Val Gly Met Gly Ala Gln Leu Leu Asp Glu Ser 2515 2520 2525 Pro Val Phe Ala Ala Arg Ile Ala Glu Cys Glu Gln Ala Leu Ser Ala 2530 2535 2540 Tyr Val Asp Trp Ser Leu Ser Asp Val Leu Arg Gly Asp Gly Ser Glu 2545 2550 2555 2560 Leu Ser Arg Val Glu Val Val Gln Pro Val Leu Trp Ala Val Met Val 2565 2570 2575 Ser Leu Ala Ala Val Trp Ala Asp Tyr Gly Val Thr Pro Ala Ala Val 2580 2585 2590 Val Gly His Ser Gln Gly Glu Met Ala Ala Ala Cys Val Ala Gly Ala 2595 2600 2605 Leu Ser Leu Glu Asp Ala Ala Arg Ile Val Ala Val Arg Ser Asp Ala 2610 2615 2620 Leu Arg Gln Leu Gln Gly His Gly Asp Met Ala Ser Leu Gly Thr Gly 2625 2630 2635 2640 Ala Glu Gln Ala Ala Glu Leu Ile Gly Asp Arg Pro Gly Val Val Val 2645 2650 2655 Ala Ala Val Asn Gly Pro Ser Ser Thr Val Ile Ser Gly Pro Pro Glu 2660 2665 2670 His Val Ala Ala Val Val Ala Glu Ala Glu Ala Arg Gly Leu Arg Ala 2675 2680 2685 Arg Val Ile Asp Val Gly Tyr Ala Ser His Gly Pro Gln Ile Asp Gln 2690 2695 2700 Leu His Asp Leu Leu Thr Glu Gly Leu Ala Asp Ile Arg Pro Ala Asn 2705 2710 2715 2720 Thr Asp Val Ala Phe Tyr Ser Thr Val Thr Ala Glu Arg Leu Thr Asp 2725 2730 2735 Thr Thr Ala Leu Asp Thr Asp Tyr Trp Val Thr Asn Leu Arg Gln Pro 2740 2745 2750 Val Arg Phe Ala Asp Thr Ile Glu Ala Leu Leu Ala Asp Gly Tyr Arg 2755 2760 2765 Leu Phe Ile Glu Ala Ser Ala His Pro Val Leu Gly Leu Gly Met Glu 2770 2775 2780 Glu Thr Ile Glu Gln Ala Asp Ile Pro Ala Thr Val Val Pro Thr Leu 2785 2790 2795 2800 Arg Arg Asp His Gly Asp Thr Thr Gln Leu Thr Arg Ala Ala Ala His 2805 2810 2815 Ala Phe Thr Ala Gly Ala Asp Val Asp Trp Arg Arg Trp Phe Pro Ala 2820 2825 2830 Asp Pro Thr Pro Arg Thr Val Asp Leu Pro Thr Tyr Ala Phe Gln His 2835 2840 2845 Gln His Tyr Trp Leu Glu Glu Pro Ser Gly Leu Thr Gly Asp Ala Ala 2850 2855 2860 Asp Leu Gly Met Val Ala Ala Gly His Pro Leu Leu Gly Ala Cys Val 2865 2870 2875 2880 Glu Leu Ala Glu Ser Asp Ser Tyr Leu Phe Thr Gly Arg Leu Ser Arg 2885 2890 2895 Arg Ala Pro Ser Trp Leu Ala Glu His Val Val Ala Gly Thr Val Leu 2900 2905 2910 Val Pro Gly Ala Ala Leu Val Glu Trp Val Leu Arg Ala Gly Asp Glu 2915 2920 2925 Ala Gly Cys Pro Thr Ile Glu Glu Leu Thr Leu Gln Ala Pro Leu Val 2930 2935 2940 Leu Pro Glu Ser Gly Gly Leu Gln Val Gln Val Val Val Gly Ala Thr 2945 2950 2955 2960 Asp Glu Gln Ser Gly Arg Arg Asp Val His Val Tyr Ser Arg Ser Glu 2965 2970 2975 Gln Asp Ala Ser Ala Val Trp Val Cys His Ala Val Gly Val Val Ser 2980 2985 2990 Ser Glu Met Pro Glu Ala Ala Ala Glu Leu Ser Gly Gln Trp Pro Pro 2995 3000 3005 Ala Gly Ala Glu Ala Val Asp Val Glu Asp Phe Tyr Ala Arg Ala Ala 3010 3015 3020 Glu Ala Gly Tyr Ala Tyr Gly Pro Ala Phe Gln Gly Leu Arg Ala Leu 3025 3030 3035 3040 Trp Arg His Gly Thr Glu Leu Phe Ala Glu Val Val Leu Pro Glu Gln 3045 3050 3055 Ala Gly Gly His Asp Gly Phe Gly Ile His Pro Ala Leu Leu Asp Ala 3060 3065 3070 Ala Leu His Pro Leu Met Leu Leu Asp Arg Pro Ala Asp Gly Gln Met 3075 3080 3085 Trp Leu Pro Phe Ala Trp Ser Gly Val Ser Leu Asn Ala Asp Arg Ala 3090 3095 3100 Thr His Val Arg Val Arg Leu Ser Pro Arg Gly Glu Ala Ala Glu Arg 3105 3110 3115 3120 Asp Leu Arg Val Val Ile Ala Asp Ala Thr Gly Ala Pro Val Leu Thr 3125 3130 3135 Val Asp Ala Leu Thr Leu Arg Ala Ala Asp Pro Gly Arg Leu Gly Ala 3140 3145 3150 Ala Ala Arg Gly Gly Val Asp Gly Leu Tyr Thr Val Asp Trp Thr Pro 3155 3160 3165 Leu Pro Leu Pro Gln Pro Leu Pro Leu Pro Arg Thr Asp Ala Gly Gly 3170 3175 3180 Ser Ala Asp Trp Val Ile Leu Ser Asp Asn Ser Ser Ala Ala Leu Ala 3185 3190 3195 3200 Asp Ala Val Ser Ser Ala Thr Ala Ala Gly Gly Gly Ala Pro Trp Ala 3205 3210 3215 Leu Leu Ala Pro Val Gly Gly Gly Ser Ala Asp Asp Gly Leu Pro Val 3220 3225 3230 Val Arg Arg Thr Leu Ser Leu Val Gln Glu Phe Leu Ala Ala Pro Glu 3235 3240 3245 Leu Thr Glu Ser Arg Leu Val Ile Val Thr Arg Gly Ala Val Ala Thr 3250 3255 3260 Asp Ala Asp Gly Asp Val Ala Ala Ser Ala Ala Ala Val Trp Gly Leu 3265 3270 3275 3280 Ile Arg Ser Ala Gln Ser Glu Asn Pro Gly Arg Phe Val Leu Leu Asp 3285 3290 3295 Val Glu Glu Glu His Leu His Pro Asp Gly Gly Glu Leu Pro Tyr Ala 3300 3305 3310 Ala Leu Arg His Ala Val Glu Glu Leu Asp Glu Pro Gln Leu Ala Leu 3315 3320 3325 Arg Ser Gly Lys Phe Leu Val Pro Arg Met Thr Pro Ala Ala Ala Pro 3330 3335 3340 Glu Glu Leu Val Pro Pro Val Gly Thr Ser Gly Trp Arg Leu Gly Thr 3345 3350 3355 3360 Ser Gly Thr Ala Thr Leu Glu Asn Leu Ser Val Ile Asp Ala Pro Glu 3365 3370 3375 Ala Phe Ala Pro Leu Glu Pro Gly Gln Val Arg Ile Ser Val Arg Ala 3380 3385 3390 Ala Gly Met Asn Phe Arg Asp Val Leu Ile Ala Leu Gly Met Tyr Pro 3395 3400 3405 Asp Lys Gly Thr Phe Ala Gly Ser Glu Gly Ala Gly His Val Thr Glu 3410 3415 3420 Val Gly Pro Gly Val Thr His Leu Ser Val Gly Asp Arg Val Met Gly 3425 3430 3435 3440 Leu Phe Glu Gly Ala Phe Ala Pro Leu Ala Val Ala Asp Ala Arg Met 3445 3450 3455 Val Val Pro Ile Pro Glu Gly Trp Ser Phe Gln Glu Ala Ala Ala Val 3460 3465 3470 Pro Val Val Phe Leu Thr Ala Trp Tyr Gly Leu Val Asp Leu Gly Arg 3475 3480 3485 Leu Arg Ala Gly Glu Ser Leu Leu Ile His Ala Gly Thr Gly Gly Val 3490 3495 3500 Gly Met Ala Ala Thr Gln Ile Ala Arg His Leu Gly Ala Glu Val Phe 3505 3510 3515 3520 Ala Thr Ala Ser Pro Ala Lys His Gly Val Leu Asp Gly Met Gly Ile 3525 3530 3535 Asp Ala Ala His Arg Ala Ser Ser Arg Asp Leu Asp Phe Glu Glu Thr 3540 3545 3550 Leu Arg Ala Ala Thr Gly Gly Arg Gly Met Asp Val Val Leu Asn Ser 3555 3560 3565 Leu Ala Gly Glu Phe Thr Asp Ala Ser Leu Arg Leu Leu Ala Glu Gly 3570 3575 3580 Gly Arg Met Val Asp Met Gly Lys Thr Asp Lys Arg Asp Pro Asp Arg 3585 3590 3595 3600 Val Ala Ala Glu His Ala Gly Ala Trp Tyr Arg Ala Phe Asp Leu Val 3605 3610 3615 Pro His Ala Gly Pro Asp Arg Ile Gly Glu Met Leu Ala Glu Leu Gly 3620 3625 3630 Glu Leu Phe Ala Ser Gly Ala Leu Ala Pro Leu Pro Val Gln Thr Trp 3635 3640 3645 Pro Leu Gly Arg Ala Arg Glu Ala Phe Arg Phe Met Ser Gln Ala Lys 3650 3655 3660 His Thr Gly Lys Leu Val Leu Glu Ile Pro Pro Ala Leu Asp Pro Asp 3665 3670 3675 3680 Gly Thr Val Leu Ile Thr Gly Gly Thr Gly Val Leu Ala Ala Ala Val 3685 3690 3695 Ala Glu His Leu Val Arg Glu Trp Gly Val Arg His Leu Leu Leu Ala 3700 3705 3710 Gly Arg Arg Gly Ser Glu Ala Pro Gly Ser Ser Glu Leu Ala Glu Glu 3715 3720 3725 Leu Thr Glu Leu Gly Ala Glu Val Thr Phe Ala Ala Ala Asp Val Ser 3730 3735 3740 Asp Pro Asp Ala Val Ala Glu Leu Val Gly Lys Thr Asp Pro Ala His 3745 3750 3755 3760 Pro Leu Thr Gly Val Ile His Ala Ala Gly Val Leu Asp Asp Ala Val 3765 3770 3775 Val Thr Ala Gln Thr Pro Glu Ser Leu Ala Arg Val Trp Ala Ala Lys 3780 3785 3790 Ala Thr Ala Ala His Leu Leu His Glu Ala Thr Arg Glu Ala Arg Leu 3795 3800 3805 Gly Leu Phe Leu Val Phe Ser Ser Ala Ala Ala Thr Leu Gly Ser Pro 3810 3815 3820 Gly Gln Ala Asn Tyr Ala Ala Ala Asn Ala Tyr Cys Asp Ala Leu Val 3825 3830 3835 3840 Arg Gln Arg Arg Ala Glu Gly Leu Ala Gly Leu Ser Ile Gly Trp Gly 3845 3850 3855 Leu Trp Gln Thr Ala Ser Gly Met Thr Gly His Leu Gly Glu Thr Asp 3860 3865 3870 Leu Ala Arg Met Lys Arg Thr Gly Phe Thr Pro Leu Thr Thr Glu Gly 3875 3880 3885 Gly Leu Ala Leu Leu Asp Ala Ala Arg Ala His Gly Arg Pro His Val 3890 3895 3900 Val Ala Val Asp Leu Asp Ala Arg Ala Val Ala Ala Gln Pro Ala Pro 3905 3910 3915 3920 Ser Arg Pro Ala Leu Leu Arg Ala Leu Ala Ala Gly Ala Thr Pro Gly 3925 3930 3935 Ala Arg Thr Ala Arg Arg Thr Ala Ala Ala Gly Ser Val Ala Pro Ala 3940 3945 3950 Gly Gly Leu Ala Asp Arg Leu Ala Gly Leu Pro His Pro Glu Arg Arg 3955 3960 3965 Arg Leu Leu Leu Asp Leu Val Arg Gly Asn Val Ala Gly Val Leu Gly 3970 3975 3980 His Ser Asp His Asp Ala Val Arg Pro Asp Thr Ser Phe Lys Glu Leu 3985 3990 3995 4000 Gly Phe Asp Ser Leu Thr Ala Val Glu Leu Arg Asn Arg Leu Ala Ala 4005 4010 4015 Ala Thr Gly Leu Lys Leu Pro Ala Ala Leu Val Phe Asp Tyr Pro Glu 4020 4025 4030 Ser Ala Thr Leu Val Asp His Leu Leu Glu Arg Leu Ser Pro Asp Gly 4035 4040 4045 Ala Pro Pro Pro Val Lys Asp Ala Ala Asp Pro Val Leu Asn Asp Leu 4050 4055 4060 Gly Arg Ile Glu Ser Ser Leu Asp Ala Leu Ala Leu Asp Ala Asp Ala 4065 4070 4075 4080 Arg Ser Arg Val Thr Arg Arg Leu Asn Thr Leu Leu Ser Lys Leu Asn 4085 4090 4095 Gly Ala Ala Thr Ala Gly Ser Pro Ala Asp Val Thr Asp Leu Asp Ala 4100 4105 4110 Leu Asp Ala Leu Asp Asp Val Ser Asp Asp Glu Met Phe Glu Phe Ile 4115 4120 4125 Asp Arg Glu Leu 4130 22 4038 PRT Streptomyces cinnamonensis 22 Met Ser Ser Ala Glu Glu Ser Ser Pro Asp Val Ser Gly Thr Gly Val 1 5 10 15 Ser Gly Thr Gly Glu Ser Ala Thr Gly Thr Ser Ser Thr Glu Ala Lys 20 25 30 Leu Arg Gln Tyr Leu Lys Arg Val Thr Val Asp Leu Gly Gln Ala Arg 35 40 45 Arg Arg Leu Arg Glu Val Glu Glu Arg Ala Gln Glu Pro Ile Ala Ile 50 55 60 Val Ser Met Ala Cys Arg Phe Pro Gly Asp Thr Arg Thr Pro Glu Ala 65 70 75 80 Leu Trp Asp Leu Val Ala Glu Gly Gly Asp Ala Ile Asp Asp Phe Pro 85 90 95 Thr Asn Arg Gly Trp Asp Leu Glu Ser Leu Tyr His Pro Asp Pro Asp 100 105 110 His Pro Gly Thr Ser Tyr Val Arg Arg Gly Gly Phe Leu Tyr Asp Ala 115 120 125 Pro Ala Phe Asp Ala Ser Phe Phe Gly Ile Ser Pro Arg Glu Ala Leu 130 135 140 Ala Met Asp Pro Gln Gln Arg Val Leu Met Glu Thr Ala Trp Gln Leu 145 150 155 160 Leu Glu Arg Ala Gly Ile Asp Pro Ala Ser Leu Lys Leu Ser Ala Thr 165 170 175 Gly Val Tyr Ile Gly Ala Gly Val Leu Gly Phe Gly Gly Ala Gln Pro 180 185 190 Asp Lys Thr Val Glu Gly His Leu Leu Thr Gly Ser Ala Leu Ser Val 195 200 205 Leu Ser Gly Arg Ile Ser Phe Thr Leu Gly Leu Glu Gly Pro Ser Val 210 215 220 Ser Val Asp Thr Ala Cys Ser Ser Ser Leu Val Ser Met His Leu Ala 225 230 235 240 Ala Gln Ala Leu Arg Gln Gly Glu Cys Asp Leu Ala Leu Ala Gly Gly 245 250 255 Val Thr Val Met Ser Thr Pro Gly Ala Phe Thr Glu Phe Ser Arg Gln 260 265 270 Gly Ala Leu Ser Pro Asp Gly Arg Ser Lys Ala Phe Ala Ala Ser Ala 275 280 285 Asp Gly Thr Gly Phe Ser Glu Gly Ala Gly Leu Leu Leu Leu Glu Arg 290 295 300 Leu Ser Asp Ala Arg Arg Asn Gly His Lys Val Leu Ala Val Ile Arg 305 310 315 320 Gly Ser Ala Val Asn Gln Asp Gly Ala Ser Asn Gly Leu Thr Ala Pro 325 330 335 Asn Gly Pro Ser Gln Glu Arg Val Ile Arg Ala Ala Leu Ala Asn Ala 340 345 350 Gly Leu Gly Ala Ala Glu Val Asp Ala Val Glu Ala His Gly Thr Gly 355 360 365 Thr Lys Leu Gly Asp Pro Ile Glu Ala Gly Ala Leu Leu Ala Thr Tyr 370 375 380 Gly Arg Asp Arg Asp Glu Asp Arg Pro Leu Trp Leu Gly Ser Val Lys 385 390 395 400 Ser Asn Ile Gly His Pro Gln Gly Ala Ala Gly Val Ala Gly Val Ile 405 410 415 Lys Met Val Met Ala Leu Gln Arg Glu Leu Leu Pro Ala Thr Leu Tyr 420 425 430 Val Asp Glu Pro Thr Pro His Val Asp Trp Ser Ser Gly Ser Val Arg 435 440 445 Leu Leu Thr Glu Pro Val Pro Trp Thr Arg Gly Glu Arg Pro Arg Arg 450 455 460 Ala Gly Val Ser Ala Phe Gly Met Ser Gly Thr Asn Ala His Val Ile 465 470 475 480 Leu Glu Glu Ala Pro Pro Glu Glu Ala Ala Ala Ala Glu Thr Pro Ala 485 490 495 Glu Gly Thr Gly Ala Val Val Pro Trp Val Val Ser Gly Arg Gly Glu 500 505 510 Glu Ala Leu Arg Ala Gln Ala Ala Gln Leu Ala Glu His Val Arg Asp 515 520 525 Asp Asp Gln Arg Pro Ala Ser Pro Leu Glu Val Gly Trp Ser Leu Ala 530 535 540 Thr Thr Arg Ser Val Phe Glu Asn Arg Ala Val Val Val Gly Asp Asp 545 550 555 560 Arg Asp Ala Leu Leu Asp Gly Leu Arg Ser Leu Ala Ala Gly Glu Ala 565 570 575 Ser Pro Asp Val Val Ser Gly Ala Val Gly Pro Thr Gly Pro Gly Pro 580 585 590 Val Met Val Phe Pro Gly Gln Gly Gly Gln Trp Val Gly Met Gly Ala 595 600 605 Arg Leu Leu Asp Glu Ser Pro Val Phe Ala Ala Arg Ile Ala Glu Cys 610 615 620 Glu Gln Ala Leu Ser Ala Tyr Val Asp Trp Ser Leu Thr Asp Val Leu 625 630 635 640 Arg Gly Asp Gly Ser Glu Leu Ala Arg Ile Asp Val Val Gln Pro Val 645 650 655 Leu Trp Ala Val Met Val Ala Leu Ala Ala Val Trp Ala Asp Gln Gly 660 665 670 Ile Glu Pro Ala Ala Val Val Gly His Ser Gln Gly Glu Ile Ala Ala 675 680 685 Ala Cys Val Val Gly Ala Ile Ser Leu Asp Glu Ala Ala Arg Ile Val 690 695 700 Ala Val Arg Ser Val Leu Leu Arg Gln Leu Ser Gly Arg Gly Gly Met 705 710 715 720 Ala Ser Leu Gly Met Gly Gln Glu Gln Ala Ala Asp Leu Ile Asp Gly 725 730 735 His Pro Gly Val Val Val Ala Ala Val Asn Gly Pro Ser Ser Thr Val 740 745 750 Ile Ser Gly Pro Pro Glu Gly Ile Ala Ala Val Val Ala Asp Ala Gln 755 760 765 Glu Arg Gly Leu Arg Ala Arg Ala Val Ala Ser Asp Val Ala Gly His 770 775 780 Gly Pro Gln Leu Asp Ala Ile Leu Asp Gln Leu Thr Glu Gly Leu Ala 785 790 795 800 Gly Ile Arg Pro Ala Ala Thr Asp Val Ala Phe Tyr Ser Thr Val Thr 805 810 815 Ala Gly His Leu Thr Asp Thr Thr Glu Leu Asp Thr Ala Tyr Trp Val 820 825 830 Arg Asn Val Arg Arg Thr Val Arg Phe Ala Asp Thr Ile Asp Ala Leu 835 840 845 Leu Ala Asp Gly Tyr Arg Leu Phe Ile Glu Val Ser Pro His Pro Val 850 855 860 Leu Asn Leu Ala Leu Glu Gly Leu Ile Glu Arg Ala Ala Val Pro Ala 865 870 875 880 Thr Val Val Pro Thr Leu Arg Arg Asp His Gly Asp Thr Thr Gln Leu 885 890 895 Ala Arg Ala Ala Ala His Ala Phe Ala Ala Gly Ala Asp Val Asp Trp 900 905 910 Arg Arg Trp Phe Pro Ala Asp Pro Ala Pro Arg Thr Val Asp Leu Pro 915 920 925 Thr Tyr Ala Phe Gln Arg Gln Asp Phe Trp Pro Ala Pro Ala Gly Gly 930 935 940 Arg Ser Gly Asp Pro Ala Gly Leu Gly Leu Ala Ala Ser Gly His Pro 945 950 955 960 Leu Leu Gly Ala Ser Val Gly Leu Ala Ser Gly Asp Val His Leu Leu 965 970 975 Ser Gly Arg Val Ser Arg Gln Ser Ala Ala Trp Leu Asp Asp His Val 980 985 990 Val Ala Gly Gln Ala Leu Val Pro Gly Ala Ala Gln Val Glu Trp Val 995 1000 1005 Leu Arg Ala Gly Asp Asp Ala Gly Cys Ser Ala Leu Glu Glu Leu Thr 1010 1015 1020 Leu Gln Thr Pro Leu Val Leu Pro Asp Thr Gly Gly Leu Arg Ile Gln 1025 1030 1035 1040 Val Val Val Glu Ala Ala Asp Ala His Gly Arg Arg Asp Val Arg Leu 1045 1050 1055 Phe Ser Arg Pro Asp Asp Asp Asp Ala Phe Ala Ser Thr His Pro Trp 1060 1065 1070 Thr Cys His Ala Thr Gly Val Leu Ala Pro Ala Pro Thr Asp Gly Thr 1075 1080 1085 Asn Gly Thr Arg Asp Ala Ala Asp Thr Leu Asp Gly Ala Trp Pro Pro 1090 1095 1100 Ala Asp Ala Glu Pro Val Pro Ala Asp Asp Leu Tyr Ala Gln Ala Asp 1105 1110 1115 1120 Arg Thr Gly Tyr Gly Tyr Gly Pro Ala Phe Arg Gly Val Arg Ala Leu 1125 1130 1135 Trp Arg His Gly Lys Asp Val Leu Ala Glu Val Thr Leu Pro Lys Glu 1140 1145 1150 Ala Gly Asp Pro Asp Gly Phe Gly Ile His Pro Ala Leu Leu Asp Ala 1155 1160 1165 Val Leu Gln Pro Ala Ala Leu Leu Leu Pro Pro Thr Asp Ala Glu Gln 1170 1175 1180 Val Trp Leu Pro Phe Ala Trp Asn Asp Val Ala Leu His Ala Val Arg 1185 1190 1195 1200 Ala Thr Thr Val Arg Val Arg Leu Thr Pro Leu Gly Glu Arg Ile Asp 1205 1210 1215 Gln Gly Leu Arg Ile Thr Val Ala Asp Ala Val Gly Ala Pro Val Leu 1220 1225 1230 Thr Val Arg Asp Leu Arg Ser Arg Pro Thr Asp Thr Gly Arg Leu Ala 1235 1240 1245 Ala Ala Ala Thr Arg Asp Arg His Gly Leu Phe Asp Leu Glu Trp Ile 1250 1255 1260 Ala Pro Glu Asn Ala Ala Glu Asn Ala Ala Gly Pro Ala Arg Asp Ala 1265 1270 1275 1280 Ser Glu Gly Trp Val Thr Leu Gly Glu Asp Ala Ala Ser Leu Ala Asp 1285 1290 1295 Leu Leu Ala Ser Val Glu Ala Gly Ala Pro Ala Pro Gln Leu Val Ala 1300 1305 1310 Ala Pro Val Glu Pro Asp Arg Thr Asp Asp Gly Leu Ala Leu Ala Thr 1315 1320 1325 His Val Leu Asp Leu Val Gln Thr Trp Leu Ala Ser Pro Leu His Asp 1330 1335 1340 Ser Arg Leu Val Leu Val Thr Arg Gly Ala Val Thr Asp Ala Asp Val 1345 1350 1355 1360 Asp Val Ala Ala Ala Ala Val Trp Gly Leu Val Arg Ser Ala Gln Ser 1365 1370 1375 Glu His Pro Gly Arg Phe Thr Leu Ile Asp Leu Gly Pro Asp Asp Thr 1380 1385 1390 Leu Ala Ala Ala Met Gln Ala Ala His Leu Glu Glu Pro Gln Leu Ala 1395 1400 1405 Val His Gly Gly Glu Ile Arg Val Pro Arg Leu Val Arg Ala Thr Thr 1410 1415 1420 Asp Pro Thr Ala Pro Asn Gly Thr Pro Glu Ala Asp Arg Thr Ala Asp 1425 1430 1435 1440 Pro Ser Glu Gly Leu His Arg Asn Gly Thr Val Leu Ile Thr Gly Gly 1445 1450 1455 Thr Gly Val Leu Gly Arg Leu Val Ala Glu His Leu Val Thr Glu Trp 1460 1465 1470 Gly Val Arg His Leu Leu Leu Ala Ser Arg Arg Gly Asp Gln Ala Pro 1475 1480 1485 Gly Ser Ala Glu Leu Arg Ala Arg Leu Ser Glu Leu Gly Ala Ser Val 1490 1495 1500 Glu Ile Ala Pro Ala Asp Val Gly Asp Ala Glu Ala Val Ala Ala Leu 1505 1510 1515 1520 Ile Ala Ser Val Asp Pro Ala His Pro Leu Thr Gly Val Ile His Ala 1525 1530 1535 Ala Gly Val Leu Asp Asp Ala Val Ile Thr Ala Gln Thr Pro Glu Ser 1540 1545 1550 Leu Ala Arg Val Trp Ala Thr Lys Ala Thr Ala Ala Arg His Leu His 1555 1560 1565 Glu Ala Thr Arg Glu Thr Pro Leu Asp Phe Phe Val Val Phe Ser Ser 1570 1575 1580 Ala Ala Ala Ser Leu Gly Ser Pro Gly Gln Ala Asn Tyr Ala Ala Ala 1585 1590 1595 1600 Asn Ala Tyr Cys Asp Ala Leu Val Gln His Arg Arg Ala Gln Gly Leu 1605 1610 1615 Ala Gly Leu Ser Ile Ala Trp Gly Leu Trp Gln Ala Thr Ser Gly Met 1620 1625 1630 Thr Gly Gln Leu Ser Glu Thr Asp Leu Ala Arg Met Lys Arg Thr Gly 1635 1640 1645 Phe Ala Ala Leu Thr Asp Glu Gly Gly Leu Ala Leu Leu Asp Ala Ala 1650 1655 1660 Arg Ala His Asp Arg Ala Tyr Val Val Ala Ala Asp Leu Asp Pro Arg 1665 1670 1675 1680 Ala Val Thr Asp Gly Leu Ser Pro Leu Leu Arg Ala Leu Thr Ala Pro 1685 1690 1695 Ala Thr Arg Arg Arg Val Ala Ser Glu Gly Leu Ala Asp Gly Ala Leu 1700 1705 1710 Ala Thr Arg Leu Ala Gly Leu Asp Ala Asp Gly Arg Leu Arg Leu Leu 1715 1720 1725 Thr Asp Val Val Arg Glu Tyr Val Ala Ala Val Leu Gly His Gly Ser 1730 1735 1740 Ala Ala Arg Val Gly Val Asp Ile Ala Phe Lys Asp Leu Gly Phe Asp 1745 1750 1755 1760 Ser Leu Thr Ala Val Glu Leu Arg Asn Arg Leu Ser Ala Ala Cys Asp 1765 1770 1775 Val Arg Leu Pro Ala Thr Leu Ile Phe Asp His Pro Thr Pro Gln Ala 1780 1785 1790 Leu Ala Thr His Leu Val Asp Arg Leu Ala Gly Ser Thr Ser Ala Thr 1795 1800 1805 Thr Thr Val Asn Ala Thr Ala Pro Ala Ala Ala His Val Ala Ala Gly 1810 1815 1820 Ala Asp Val Asp Ala Asp Thr Asp Asp Pro Val Ala Ile Val Ala Met 1825 1830 1835 1840 Thr Cys Arg Phe Pro Gly Gly Val Ala Ser Pro Asp Asp Leu Trp Asp 1845 1850 1855 Leu Leu Asp Ala Arg Lys Asp Ala Met Gly Ala Phe Pro Thr Asp Arg 1860 1865 1870 Gly Trp Asp Leu Glu Arg Leu Phe His Pro Asp Pro Asp His Pro Gly 1875 1880 1885 Thr Ser Tyr Thr Asp Gln Gly Gly Phe Leu Pro Asp Ala Gly Asp Phe 1890 1895 1900 Asp Ala Ala Phe Phe Gly Ile Asn Pro Arg Glu Ala Leu Ala Met Asp 1905 1910 1915 1920 Pro Gln Gln Arg Leu Leu Leu Glu Ala Ser Trp Glu Val Leu Glu Arg 1925 1930 1935 Ala Gly Ile Asp Pro Thr Thr Leu Lys Gly Thr Pro Thr Gly Thr Tyr 1940 1945 1950 Val Gly Leu Met Tyr His Asp Tyr Ala Lys Ser Phe Pro Thr Ala Asp 1955 1960 1965 Ala Gln Leu Glu Gly Tyr Ser Tyr Leu Ala Ser Thr Gly Ser Met Val 1970 1975 1980 Ser Gly Arg Val Ala Tyr Thr Leu Gly Leu Glu Gly Pro Ala Val Thr 1985 1990 1995 2000 Val Asp Thr Ala Cys Ser Ser Ser Leu Val Ser Ile His Leu Ala Thr 2005 2010 2015 Gln Ala Leu Arg His Gly Glu Cys Asp Leu Ala Leu Ala Gly Gly Val 2020 2025 2030 Thr Val Met Ala Asp Pro Asp Met Phe Ala Gly Phe Ser Arg Gln Arg 2035 2040 2045 Gly Leu Ser Pro Asp Gly Arg Cys Lys Ala Tyr Ala Ala Ala Ala Asp 2050 2055 2060 Gly Val Gly Phe Ser Glu Gly Val Gly Val Leu Leu Leu Glu Arg Leu 2065 2070 2075 2080 Ser Asp Ala Arg Arg His Gly Arg Arg Val Leu Gly Val Val Arg Gly 2085 2090 2095 Ser Ala Val Asn Gln Asp Gly Ala Ser Asn Gly Leu Thr Ala Pro Asn 2100 2105 2110 Gly Pro Ser Gln Glu Arg Val Ile Arg Gln Ala Leu Ala Ser Gly Gly 2115 2120 2125 Leu Ser Ser Val Asp Val Asp Val Val Glu Gly His Gly Thr Gly Thr 2130 2135 2140 Thr Leu Gly Asp Pro Ile Glu Ala Gln Ala Leu Leu Ala Thr Tyr Gly 2145 2150 2155 2160 Gln Gly Arg Pro Glu Asp Arg Pro Leu Trp Leu Gly Ser Val Lys Ser 2165 2170 2175 Asn Ile Gly His Thr Gln Ala Ala Ala Gly Val Ala Gly Val Ile Lys 2180 2185 2190 Met Val Met Ala Met Arg His Gly Val Val Pro Ala Ser Leu His Val 2195 2200 2205 Asp Val Pro Ser Pro His Val Glu Trp Asp Ser Gly Ala Val Arg Leu 2210 2215 2220 Ala Val Glu Ser Val Pro Trp Pro Gln Val Glu Gly Arg Pro Arg Arg 2225 2230 2235 2240 Ala Gly Val Ser Ser Phe Gly Ala Ser Gly Thr Asn Ala His Val Ile 2245 2250 2255 Val Glu Ser Val Pro Asp Gly Leu Glu Glu Asp Ser Val Ser Val Gly 2260 2265 2270 Gly Glu Ala Leu Glu Thr Glu Thr Asp Gly Arg Leu Val Pro Trp Val 2275 2280 2285 Val Ser Ala Arg Ser Pro Gln Ala Leu Arg Asp Gln Ala Leu Arg Leu 2290 2295 2300 Arg Asp Phe Ala Ser Asp Ala Ser Phe Arg Ala Pro Leu Ala Asp Val 2305 2310 2315 2320 Gly Trp Ser Leu Leu Lys Thr Arg Ala Leu His Glu His Arg Ala Val 2325 2330 2335 Val Val Gly Ala Glu Arg Ala Glu Leu Ile Ala Ala Leu Glu Ala Leu 2340 2345 2350 Ala Thr Gly Glu Pro His Ala Ala Leu Val Gly Pro Ala Cys Ser Gln 2355 2360 2365 Ala Arg Val Gly Gly Asp Asp Val Val Trp Leu Phe Ser Gly Gln Gly 2370 2375 2380 Ser Gln Leu Val Gly Met Gly Ala Gly Leu Tyr Glu Arg Phe Pro Val 2385 2390 2395 2400 Phe Ala Ala Ala Phe Asp Glu Val Cys Gly Leu Leu Glu Gly Pro Leu 2405 2410 2415 Gly Val Glu Ala Gly Gly Leu Arg Glu Val Val Phe Arg Gly Pro Arg 2420 2425 2430 Glu Arg Leu Asp His Thr Val Trp Ala Gln Ala Gly Leu Phe Ala Leu 2435 2440 2445 Gln Val Gly Leu Ala Arg Leu Trp Glu Ser Val Gly Val Arg Pro Asp 2450 2455 2460 Val Val Leu Gly His Ser Ile Gly Glu Ile Ala Ala Ala His Val Ala 2465 2470 2475 2480 Gly Val Phe Asp Leu Ala Asp Ala Cys Arg Val Val Gly Ala Arg Ala 2485 2490 2495 Arg Leu Met Gly Gly Leu Pro Glu Gly Gly Ala Met Cys Ala Val Gln 2500 2505 2510 Ala Thr Pro Ala Glu Leu Ala Ala Asp Val Asp Gly Ser Ala Val Ser 2515 2520 2525 Val Ala Ala Val Asn Thr Pro Asp Ser Thr Val Ile Ser Gly Pro Ser 2530 2535 2540 Asp Glu Val Asp Arg Ile Ala Gly Val Trp Arg Glu Arg Gly Arg Lys 2545 2550 2555 2560 Thr Lys Ala Leu Ser Val Ser His Ala Phe His Ser Ala Leu Met Glu 2565 2570 2575 Pro Met Leu Ala Glu Phe Thr Glu Ala Ile Arg Gly Val Lys Phe Arg 2580 2585 2590 Gln Pro Ser Ile Pro Leu Met Ser Asn Val Ser Gly Glu Arg Ala Gly 2595 2600 2605 Glu Glu Ile Thr Asp Pro Glu Tyr Trp Ala Arg His Val Arg Asn Ala 2610 2615 2620 Val Leu Phe Gln Pro Ala Ile Ala Gln Val Ala Asp Ser Ala Gly Val 2625 2630 2635 2640 Phe Val Glu Leu Gly Pro Ala Pro Val Leu Thr Thr Ala Ala Gln His 2645 2650 2655 Thr Leu Asp Glu Ser Asp Ser Gln Glu Ser Val Leu Val Ala Ser Leu 2660 2665 2670 Ala Gly Glu Arg Pro Glu Glu Ser Ala Phe Val Glu Ala Met Ala Arg 2675 2680 2685 Leu His Thr Ala Gly Val Ala Val Asp Trp Ser Val Leu Phe Ala Gly 2690 2695 2700 Asp Arg Val Pro Gly Leu Val Glu Leu Pro Thr Tyr Ala Phe Gln Arg 2705 2710 2715 2720 Glu Arg Phe Trp Leu Ser Gly Arg Ser Gly Gly Gly Asp Ala Ala Thr 2725 2730 2735 Leu Gly Leu Val Ala Ala Gly His Pro Leu Leu Gly Ala Ala Val Glu 2740 2745 2750 Phe Ala Asp Arg Gly Gly Cys Leu Leu Thr Gly Arg Leu Ser Arg Ser 2755 2760 2765 Gly Val Ser Trp Leu Ala Asp His Val Val Ala Gly Ala Val Leu Val 2770 2775 2780 Pro Gly Ala Ala Leu Val Glu Trp Ala Leu Arg Ala Gly Asp Glu Val 2785 2790 2795 2800 Gly Cys Val Thr Val Glu Glu Leu Met Leu Gln Ala Pro Leu Val Val 2805 2810 2815 Pro Glu Ala Ser Gly Leu Arg Val Gln Val Val Val Glu Glu Ala Gly 2820 2825 2830 Glu Asp Gly Arg Arg Gly Val Gln Ile Tyr Ser Arg Pro Asp Ala Asp 2835 2840 2845 Ala Val Gly Gly Asp Asp Ser Trp Ile Cys His Ala Thr Gly Val Leu 2850 2855 2860 Ser Pro Glu Ser Ala Arg Leu Asp Thr Glu Leu Gly Gly Val Trp Pro 2865 2870 2875 2880 Pro Ala Gly Ala Glu Pro Leu Asp Val Asp Gly Phe Tyr Ala Gln Ala 2885 2890 2895 Gly Glu Ala Gly Tyr Gly Tyr Gly Pro Ala Phe Arg Gly Leu Arg Ala 2900 2905 2910 Val Trp Arg His Gly Gln Asp Leu Leu Ala Glu Val Val Leu Pro Glu 2915 2920 2925 Ala Ala Gly Ala His Asp Gly Tyr Gly Ile His Pro Ala Leu Leu Asp 2930 2935 2940 Ala Thr Leu His Pro Leu Leu Ala Ala Arg Phe Met Asp Gly Ser Glu 2945 2950 2955 2960 Asp Asp Gln Leu Tyr Val Pro Phe Gly Trp Ala Gly Val Ser Leu Arg 2965 2970 2975 Ala Val Gly Ala Thr Thr Val Arg Val Arg Leu Arg Pro Val Gly Glu 2980 2985 2990 Ser Val Asp Gln Gly Leu Ser Val Thr Val Thr Asp Ala Thr Gly Gly 2995 3000 3005 Pro Val Leu Ser Val Asp Ser Leu Gln Thr Arg Pro Val Lys Pro Ser 3010 3015 3020 Gln Leu Ala Ala Ala Gln Gln Pro Asp Val Arg Gly Leu Phe Thr Val 3025 3030 3035 3040 Glu Trp Thr Pro Leu Pro Gln Thr Asp Ala Asp Gly Glu Ala Asp Trp 3045 3050 3055 Val Val Leu Ser Asp Gly Val Gly Arg Leu Ala Asp Val Val Ser Ala 3060 3065 3070 Ala Gly Gly Glu Ala Pro Trp Ala Val Val Ala Pro Val Asp Ala Ser 3075 3080 3085 Val Gly Asp Gly Arg Glu Gly Leu Asp Gly Arg Leu Val Val Glu Arg 3090 3095 3100 Val Leu Ser Leu Val Gln Glu Phe Leu Ala Leu Pro Glu Leu Ala Glu 3105 3110 3115 3120 Ser Arg Leu Leu Val Val Thr Arg Gly Ala Val Ala Thr Gly Val Asp 3125 3130 3135 Gly Asp Gly Asp Val Asp Ala Ser Ala Ala Ala Val Trp Gly Leu Val 3140 3145 3150 Arg Ser Ala Gln Ser Glu Asn Pro Gly Arg Phe Ile Leu Leu Asp Val 3155 3160 3165 Asp Gly Asp Gly Asp Asp Gln Gly Pro Asp Leu Asn Gly Arg His Leu 3170 3175 3180 Pro His Ala Thr Leu Arg His Ala Ala Glu Glu Leu Asp Glu Pro Gln 3185 3190 3195 3200 Leu Ala Leu Arg Glu Gly Thr Leu Tyr Val Pro Arg Leu Thr Gln Ala 3205 3210 3215 Arg Gln Ser Ala Glu Leu Val Val Pro Pro Gly Glu Pro Ala Trp Arg 3220 3225 3230 Leu Arg Met Val His Asp Gly Ser Leu Asp Ala Leu Ala Ala Val Ala 3235 3240 3245 Cys Pro Glu Ala Leu Glu Pro Leu Ala Pro Gly Gln Val Arg Ile Ala 3250 3255 3260 Val His Ala Ala Gly Ile Asn Phe Arg Asp Val Leu Val Ala Leu Gly 3265 3270 3275 3280 Met Val Pro Ala Tyr Gly Ala Met Gly Gly Glu Gly Ala Gly Val Val 3285 3290 3295 Thr Glu Val Gly Pro Glu Val Thr His Val Ser Val Gly Asp Arg Val 3300 3305 3310 Met Gly Val Phe Glu Gly Ala Phe Gly Pro Val Val Ile Ala Glu Ala 3315 3320 3325 Arg Met Val Thr Pro Val Pro Gln Gly Trp Asp Met Arg Glu Ala Ala 3330 3335 3340 Gly Ile Pro Ala Ala Phe Leu Thr Ala Trp Tyr Gly Leu Val Glu Leu 3345 3350 3355 3360 Ala Gly Leu Lys Ala Gly Glu Arg Val Leu Val His Ala Ala Thr Gly 3365 3370 3375 Gly Val Gly Met Ala Ala Val Gln Ile Ala Arg His Val Gly Ala Glu 3380 3385 3390 Val Phe Ala Thr Ala Ser Pro Gly Lys His Ala Val Leu Glu Glu Met 3395 3400 3405 Gly Ile Asp Ala Ala His Arg Ala Ser Ser Arg Asp Leu Ala Phe Glu 3410 3415 3420 Gly Thr Phe Arg Glu Ala Thr Gly Gly Arg Gly Met Asp Val Val Leu 3425 3430 3435 3440 Asn Ser Leu Ala Gly Glu Phe Ile Asp Ala Ser Leu Arg Leu Leu Gly 3445 3450 3455 Asp Gly Gly Arg Phe Leu Glu Met Gly Lys Thr Asp Val Arg Ala Ala 3460 3465 3470 Glu Glu Val Ala Ala Glu His Ala Asp Val Ser Tyr Thr Ala Tyr Asp 3475 3480 3485 Leu Val Gly Asp Ala Gly Pro Asp Arg Ile Ser Asn Met Leu Asp Lys 3490 3495 3500 Leu Val Glu Leu Phe Ala Ser Glu Arg Leu Lys Pro Leu Pro Val Arg 3505 3510 3515 3520 Ser Trp Pro Leu Asp Lys Ala Gln Glu Ala Phe Arg Phe Met Ser Gln 3525 3530 3535 Ala Lys His Thr Gly Lys Leu Val Leu Glu Ile Pro Pro Ala Leu Asp 3540 3545 3550 Pro Glu Gly Thr Val Leu Val Thr Gly Gly Thr Gly Ala Leu Gly Gln 3555 3560 3565 Val Val Ala Glu His Leu Val Arg Glu Trp Gly Val Arg His Leu Leu 3570 3575 3580 Leu Ala Ser Arg Arg Gly Pro Glu Ala Pro Gly Ser Asp Glu Leu Ala 3585 3590 3595 3600 Ser Lys Leu Thr Gly Leu Gly Ala Glu Val Thr Ile Val Ala Ala Asp 3605 3610 3615 Val Ser Asp Pro Ala Ser Val Val Glu Leu Val Gly Lys Thr Asp Pro 3620 3625 3630 Ser His Pro Leu Thr Gly Val Val His Ala Ala Gly Val Leu Glu Asp 3635 3640 3645 Gly Val Val Thr Ala Gln Thr Pro Glu Gly Leu Ala Arg Val Trp Ala 3650 3655 3660 Ala Lys Ala Ala Ala Ala Ala Asn Leu His Glu Ala Thr Arg Glu Met 3665 3670 3675 3680 Arg Leu Gly Leu Phe Val Val Phe Ser Ser Ala Ala Ala Thr Leu Gly 3685 3690 3695 Ser Pro Gly Gln Ala Asn Tyr Ala Ala Ala Asn Ala Tyr Cys Asp Ala 3700 3705 3710 Leu Met Gln His Arg Arg Ala Val Gly Gln Val Gly Leu Ser Val Gly 3715 3720 3725 Trp Gly Leu Trp Glu Ala Pro Asp Ala Lys Pro Gly Val Ala Ala Asp 3730 3735 3740 Ala Lys Ala Ser Ala Ala Thr Val Gly Lys Ala Ser Ala Leu Ser Asp 3745 3750 3755 3760 Gly Thr Asn Gly Ser Ala Pro Gln Asp Thr Thr Gly Thr Ala Pro Gln 3765 3770 3775 Gly Met Thr Gly Gly Leu Thr Asp Thr Asp Val Ala Arg Met Ala Arg 3780 3785 3790 Ile Gly Val Lys Gly Met Ser Asn Ala His Gly Leu Ala Leu Phe Asp 3795 3800 3805 Ala Ala His Arg His Gly Arg Pro His Leu Val Gly Phe Asn Leu Asp 3810 3815 3820 Leu Arg Thr Leu Ala Thr His Pro Leu His Thr Arg Pro Ala Leu Leu 3825 3830 3835 3840 Arg Gly Leu Ala Thr Pro Thr Ala Gly Gly Ala Ser Arg Pro Thr Ala 3845 3850 3855 Thr Ala Gly Gly Gln Pro Ala Asp Leu Ala Gly Arg Leu Ala Ala Leu 3860 3865 3870 Ser Pro Ser Asp Arg His His Thr Leu Val Arg Leu Ile Arg Glu Gln 3875 3880 3885 Ala Ala Thr Val Leu Gly His His Pro Asp Ser Leu Thr Thr Gly Ser 3890 3895 3900 Thr Phe Lys Glu Leu Gly Phe Asp Ser Leu Thr Ala Val Glu Leu Arg 3905 3910 3915 3920 Asn Arg Leu Ser Ala Ala Thr Gly Leu Arg Leu Pro Ala Gly Leu Val 3925 3930 3935 Phe Asp His Pro Asp Ala Asp Ile Leu Ala Glu His Leu Gly Ala Gln 3940 3945 3950 Leu Ala Pro Asp Gly Asp Thr Pro Ala Gly Ala Glu Ala Thr Asp Pro 3955 3960 3965 Val Leu Arg Asp Leu Ala Lys Leu Glu Asn Ala Leu Ser Ser Thr Leu 3970 3975 3980 Val Glu His Leu Asp Ala Asp Ala Val Thr Ala Arg Leu Glu Ala Leu 3985 3990 3995 4000 Leu Ser Asn Trp Lys Ala Ala Ser Ala Ala Pro Gly Ser Gly Ser Thr 4005 4010 4015 Lys Glu Gln Leu Gln Val Ala Thr Thr Asp Gln Val Leu Asp Phe Ile 4020 4025 4030 Asp Lys Glu Leu Gly Val 4035 23 4106 PRT Streptomyces cinnamonensis 23 Met Ala Ser Glu Glu Glu Leu Val Asp Tyr Leu Lys Arg Val Ala Ala 1 5 10 15 Glu Leu His Asp Thr Arg Gln Arg Leu Arg Glu Val Glu Asp Arg Arg 20 25 30 Gln Glu Pro Val Ala Val Val Gly Met Ala Cys Arg Phe Pro Gly Gly 35 40 45 Ile Glu Thr Pro Glu Gly Leu Trp Glu Leu Val Ala Ala Gly Asp Asp 50 55 60 Ala Ile Glu Pro Phe Pro Thr Asp Arg Gly Trp Asp Leu Glu Gly Ile 65 70 75 80 Tyr His Pro Asp Pro Asp His Pro Gly Thr Cys Tyr Val Arg Glu Gly 85 90 95 Gly Phe Leu Ala Ala Pro Asp Arg Phe Asp Ser Asp Phe Phe Gly Phe 100 105 110 Ser Pro Arg Glu Ala Leu Ala Ser Ser Pro Gln Leu Arg Leu Leu Leu 115 120 125 Glu Thr Ser Trp Glu Ala Leu Glu Arg Ala Gly Ile Asn Pro Ala Ser 130 135 140 Leu Lys Gly Ser Pro Thr Gly Val Tyr Val Gly Ala Ala Thr Thr Gly 145 150 155 160 Asn Gln Thr Gln Gly Asp Pro Gly Gly Lys Ala Thr Glu Gly Tyr Ala 165 170 175 Gly Thr Ala Pro Ser Val Leu Ser Gly Arg Leu Ser Phe Thr Leu Gly 180 185 190 Leu Glu Gly Pro Ala Val Thr Val Glu Thr Ala Cys Ser Ser Ser Leu 195 200 205 Val Ala Met His Leu Ala Ala Asn Ala Leu Arg Gln Gly Glu Cys Asp 210 215 220 Leu Ala Leu Ala Gly Gly Val Thr Val Met Ser Thr Pro Glu Val Phe 225 230 235 240 Thr Gly Phe Ser Arg Gln Arg Gly Leu Ala Pro Asp Gly Arg Cys Lys 245 250 255 Pro Phe Ala Ala Ala Ala Asp Gly Thr Gly Trp Gly Glu Gly Ala Gly 260 265 270 Leu Ile Leu Leu Glu Arg Leu Ser Asp Ala Arg Arg Lys Gly His Lys 275 280 285 Val Leu Ala Val Ile Arg Gly Ser Ala Ile Asn Gln Asp Gly Ala Ser 290 295 300 Asn Gly Phe Thr Ala Pro Asn Gly Pro Ser Gln Arg Arg Val Ile Arg 305 310 315 320 Gln Ala Leu Ser Ser Ala His Leu Ser Thr Ser Glu Ile Asp Val Val 325 330 335 Glu Ala His Gly Thr Gly Thr Arg Leu Gly Asp Pro Ile Glu Ala Glu 340 345 350 Ala Leu Ile Ala Thr Tyr Gly Lys Glu Arg Glu Asp Asp Arg Pro Leu 355 360 365 Trp Leu Gly Ser Val Lys Ser Asn Ile Gly His Thr Gln Ala Ala Ala 370 375 380 Gly Val Ala Gly Val Ile Lys Met Val Met Ala Leu Gln Arg Glu Leu 385 390 395 400 Leu Pro Ala Thr Leu Asn Val Asp Glu Pro Thr Pro His Val Gln Trp 405 410 415 Glu Gly Gly Gly Val Arg Leu Leu Thr Glu Pro Val Pro Trp Ser Arg 420 425 430 Gly Glu Arg Pro Arg Arg Ala Gly Ile Ser Ser Phe Gly Ile Ser Gly 435 440 445 Thr Asn Ala His Val Val Leu Glu Glu Ala Pro Pro Glu Glu Asp Val 450 455 460 Pro Gly Pro Val Ala Ala Glu Pro Glu Gly Val Val Pro Trp Val Val 465 470 475 480 Ser Ala Arg Thr Glu Glu Ala Leu Ser Glu Gln Ala Arg Arg Leu Gly 485 490 495 Glu Phe Val Ala Asp Thr Asp Pro Ser Thr Ala Asp Val Gly Trp Ser 500 505 510 Leu Thr Thr Ser Arg Ala Ile Leu Glu His Arg Ala Val Val Val Gly 515 520 525 Arg Asp Arg Asp Ala Leu Thr Ala Gly Leu Ala Ala Leu Ala Ala Gly 530 535 540 Glu Glu Ser Ala Asp Val Val Ala Gly Val Ala Gly Asp Val Gly Pro 545 550 555 560 Gly Pro Val Leu Val Phe Pro Gly Gln Gly Ser Gln Trp Val Gly Met 565 570 575 Gly Ala Gln Leu Leu Asp Glu Ser Pro Val Phe Ala Ala Arg Ile Ala 580 585 590 Glu Cys Glu Gln Ala Leu Ser Ala Tyr Val Asp Trp Ser Leu Ser Ala 595 600 605 Val Leu Arg Gly Asp Gly Ser Glu Leu Ser Arg Val Glu Val Val Gln 610 615 620 Pro Val Leu Trp Ala Val Met Val Ser Leu Ala Ala Val Trp Ala Asp 625 630 635 640 Tyr Gly Val Thr Pro Ala Ala Val Ile Gly His Ser Gln Gly Glu Met 645 650 655 Ala Ala Ala Cys Val Ala Gly Ala Leu Ser Leu Glu Asp Ala Ala Arg 660 665 670 Val Val Ala Val Arg Ser Asp Ala Leu Arg Gln Leu Met Gly Gln Gly 675 680 685 Asp Met Ala Ser Leu Gly Ala Ser Ser Glu Gln Ala Ala Glu Leu Ile 690 695 700 Gly Asp Arg Pro Gly Val Cys Ile Ala Ala Val Asn Gly Pro Ser Ser 705 710 715 720 Thr Val Ile Ser Gly Pro Pro Glu His Val Ala Ala Val Val Ala Asp 725 730 735 Ala Glu Glu Arg Gly Leu Arg Ala Arg Val Ile Asp Val Gly Tyr Ala 740 745 750 Ser His Gly Pro Gln Ile Asp Gln Leu His Asp Leu Leu Thr Asp Arg 755 760 765 Leu Ala Asp Ile Arg Pro Ala Thr Thr Asp Val Ala Phe Tyr Ser Thr 770 775 780 Val Thr Ala Glu Arg Leu Thr Asp Thr Thr Ala Leu Asp Thr Asp Tyr 785 790 795 800 Trp Val Thr Asn Leu Arg Gln Pro Val Arg Phe Ala Asp Thr Ile Asp 805 810 815 Ala Leu Leu Ala Asp Gly Tyr Arg Leu Phe Ile Glu Ala Ser Ala His 820 825 830 Pro Val Leu Gly Leu Gly Met Glu Glu Thr Ile Glu Gln Ala Asp Ile 835 840 845 Pro Ala Thr Val Val Pro Thr Leu Arg Arg Asp His Gly Asp Thr Thr 850 855 860 Gln Leu Thr Arg Ala Ala Ala His Ala Phe Thr Ala Gly Ala Thr Val 865 870 875 880 Asp Trp Arg Arg Trp Phe Pro Ala Asp Pro Thr Pro Arg Thr Ile Asp 885 890 895 Leu Pro Thr Tyr Ala Phe Gln Arg Arg Ser Tyr Trp Leu Pro Val Asp 900 905 910 Gly Val Gly Asp Val Arg Ser Ala Gly Leu Arg Arg Val Glu His Ser 915 920 925 Leu Leu Pro Ala Ala Leu Gly Leu Ala Asp Gly Ala Leu Val Leu Thr 930 935 940 Gly Arg Leu Ala Ala Ser Gly Gly Gly Gly Gly Trp Leu Ala Asp His 945 950 955 960 Ala Val Ala Gly Thr Thr Leu Val Pro Gly Ala Ala Leu Val Glu Trp 965 970 975 Ala Leu Arg Ala Ala Asp Glu Ala Gly Cys Pro Ser Leu Glu Glu Leu 980 985 990 Thr Leu Gln Ala Pro Leu Val Leu Pro Gly Ser Gly Gly Leu Gln Val 995 1000 1005 Gln Val Val Val Gly Pro Ala Asp Gly Gln Gly Gly Arg Arg Glu Val 1010 1015 1020 Arg Val Phe Ser Arg Val Asp Ser Asp Asp Glu Ala Ala Gly Gln Asp 1025 1030 1035 1040 Glu Gly Trp Ser Cys His Ala Thr Gly Val Leu Ser Pro Glu Pro Gly 1045 1050 1055 Ala Val Pro Asp Gly Leu Ser Gly Gln Trp Pro Pro Thr Gly Ala Glu 1060 1065 1070 Pro Leu Glu Ile Ser Asp Leu Tyr Glu Gln Ala Ala Ser Ala Gly Tyr 1075 1080 1085 Glu Tyr Gly Pro Ser Phe Arg Gly Leu Arg Ser Val Trp Arg His Gly 1090 1095 1100 His Asn Leu Leu Ala Glu Val Glu Leu Pro Glu Gln Ala Gly Ala His 1105 1110 1115 1120 Asp Asp Phe Gly Ile His Pro Val Leu Leu Asp Ala Ala Leu His Pro 1125 1130 1135 Ala Leu Leu Leu Asp Gln Asn Ala Pro Gly Glu Glu Gln Glu Pro Ala 1140 1145 1150 Gln Pro Ala Leu Arg Leu Pro Phe Val Trp Asn Gly Val Ser Leu Trp 1155 1160 1165 Ala Thr Gly Ala Ala Thr Val Arg Val Arg Leu Ala Pro His Gly Gly 1170 1175 1180 Gly Glu Thr Asp Asp Ser Ala Gly Leu Arg Val Thr Val Ala Asp Ala 1185 1190 1195 1200 Thr Gly Ala Pro Val Leu Ser Val Asp Ser Leu Ala Leu Arg Pro Ala 1205 1210 1215 Asp Pro Glu Leu Leu Arg Thr Ala Gly Arg Ala Gly Ser Gly Thr Asn 1220 1225 1230 Gly Leu Phe Thr Val Glu Trp Thr Ala Leu Pro Pro Ala Asp Val Ala 1235 1240 1245 Asp His Ala Ala Gly Asp Gly Trp Ala Val Leu Gly Gln Asp Val Pro 1250 1255 1260 Asp Trp Ala Gly Ala Asp Met Pro Arg His Pro Asp Met Ala Ser Leu 1265 1270 1275 1280 Ser Ala Ala Leu Asp Glu Gly Thr Gln Ala Pro Ala Ala Val Phe Val 1285 1290 1295 Glu Thr Thr Ala Thr Ser His Ala Thr Pro Asn Thr Ala Ala Asp Val 1300 1305 1310 Thr Leu Asp Ala Ser Gly Arg Ala Val Ala Glu Arg Thr Leu His Leu 1315 1320 1325 Leu Arg Asp Trp Leu Ala Glu Pro Arg Leu Ala Glu Thr Arg Leu Val 1330 1335 1340 Leu Ile Thr His His Ala Val Thr Thr Pro Ala Asp Asp Asp Val Asn 1345 1350 1355 1360 Ala Ala Pro Leu Asp Val Pro Ala Ala Ala Leu Trp Gly Leu Ile Arg 1365 1370 1375 Ser Ala Gln Ala Glu His Pro Asp Arg Phe Val Leu Leu Asp Thr Asp 1380 1385 1390 Ala Lys Ala Asn Thr Asp Pro Gly Pro Asp Thr Ser Thr Asp His Ser 1395 1400 1405 Thr Ala Ser Gly Thr Tyr Arg Thr Val Ile Ala Arg Ala Leu Ala Thr 1410 1415 1420 Gly Glu Pro Gln Leu Ala Val Arg Ala Gly Glu Leu Leu Ala Pro Arg 1425 1430 1435 1440 Leu Ala Arg Ala Ala Thr Pro Thr Pro Glu Thr Pro Thr Pro Glu Thr 1445 1450 1455 Gln Pro Asp Thr Gly Ser Gly Ser Glu Ala Gly Ala Gly Ser Gly Ser 1460 1465 1470 Gly Pro Gly Ala Thr Leu Asp Pro Asp Gly Thr Val Leu Ile Ala Gly 1475 1480 1485 Gly Thr Gly Met Met Gly Gly Leu Val Ala Glu His Leu Val Arg Ala 1490 1495 1500 Trp Ser Val Arg His Leu Leu Leu Val Ser Arg Gln Gly Pro Asp Ala 1505 1510 1515 1520 Pro Asp Ala Arg Asp Leu Ala Asp Arg Leu Val Gly Leu Gly Ala Thr 1525 1530 1535 Val Arg Ile Val Ala Ala Asp Leu Thr Asp Gly Arg Ala Thr Ala Asp 1540 1545 1550 Leu Val Ala Ser Val Asp Pro Ala His Pro Leu Thr Gly Val Ile His 1555 1560 1565 Ala Ala Gly Val Leu Asp Asp Ala Val Val Thr Ala Gln Thr Ser Asp 1570 1575 1580 Gln Leu Ala Arg Val Trp Ala Ala Lys Ala Ser Val Ala Ala Asn Leu 1585 1590 1595 1600 Asp Ala Ala Thr Ser Glu Leu Pro Leu Gly Leu Phe Leu Met Phe Ser 1605 1610 1615 Ser Ala Ala Gly Val Leu Gly Asn Ala Gly Gln Ala Gly Tyr Ala Ala 1620 1625 1630 Ala Asn Ala Phe Val Asp Ala Leu Val Gly Arg Arg Arg Ala Thr Gly 1635 1640 1645 Leu Pro Gly Leu Ser Ile Ala Trp Gly Leu Trp Ala Arg Gly Ser Ala 1650 1655 1660 Met Thr Arg His Leu Asp Asp Ala Asp Leu Ala Arg Leu Arg Ala Gly 1665 1670 1675 1680 Gly Val Lys Pro Leu Leu Asp Glu Gln Gly Leu Ala Leu Leu Asp Ala 1685 1690 1695 Ala Arg Ala Thr Ala Ala His Thr Ser Leu Val Val Ala Ala Gly Ile 1700 1705 1710 Asp Val Arg Gly Leu Asn Arg Asp Asp Val Pro Ala Ile Leu Arg Asp 1715 1720 1725 Leu Ala Gly Arg Thr Arg Arg Arg Ala Ala Ala Asp Ser Thr Val Asp 1730 1735 1740 Gln Ala Ala Leu Glu Arg Arg Leu Thr Gly Leu Asp Glu Ala Glu Arg 1745 1750 1755 1760 Arg Ala Val Val Thr Asp Val Val Arg Glu Cys Val Ala Ala Val Leu 1765 1770 1775 Gly His Arg Ser Ala Ala Asp Val Arg Thr Glu Ala Asn Phe Lys Asp 1780 1785 1790 Leu Gly Phe Asp Ser Leu Thr Ala Val Gln Leu Arg Asn Arg Leu Ser 1795 1800 1805 Ala Ala Ser Gly Leu Arg Leu Pro Ala Thr Leu Ala Phe Asp His Pro 1810 1815 1820 Thr Pro Gln Ala Leu Ala Ala Tyr Leu Gly Thr Arg Leu Ser Gly Arg 1825 1830 1835 1840 Thr Ala Thr Pro Val Ala Pro Val Ala Pro Ser Ala Ala Ala Thr Asp 1845 1850 1855 Glu Pro Val Ala Ile Val Ala Met Ala Cys Lys Tyr Pro Gly Gly Ala 1860 1865 1870 Thr Ser Pro Glu Gly Leu Trp Asp Leu Val Ala Glu Gly Val Asp Ala 1875 1880 1885 Val Gly Ala Phe Pro Thr Gly Arg Gly Trp Asp Leu Glu Arg Leu Phe 1890 1895 1900 His Pro Asp Pro Asp His Pro Gly Thr Ser Tyr Ala Asp Glu Gly Ala 1905 1910 1915 1920 Phe Leu Pro Asp Ala Gly Asp Phe Asp Ala Ala Phe Phe Gly Ile Asn 1925 1930 1935 Pro Arg Glu Ala Leu Ala Met Asp Pro Gln Gln Arg Leu Leu Leu Glu 1940 1945 1950 Ala Ser Trp Glu Val Leu Glu Arg Ala Gly Ile Asp Pro Thr Thr Leu 1955 1960 1965 Lys Gly Thr Pro Thr Gly Thr Tyr Val Gly Val Met Tyr His Asp Tyr 1970 1975 1980 Ala Ala Gly Leu Ala Gln Asp Ala Gln Leu Glu Gly Tyr Ser Met Leu 1985 1990 1995 2000 Ala Gly Ser Gly Ser Val Val Ser Gly Arg Val Ala Tyr Thr Leu Gly 2005 2010 2015 Leu Glu Gly Pro Ala Val Thr Val Asp Thr Ala Cys Ser Ser Ser Leu 2020 2025 2030 Val Ser Ile His Leu Ala Ala Gln Ala Leu Arg Gln Gly Glu Cys Thr 2035 2040 2045 Leu Ala Leu Ala Gly Gly Val Thr Val Met Ala Thr Pro Glu Val Phe 2050 2055 2060 Thr Gly Phe Ser Arg Gln Arg Gly Leu Ala Pro Asp Gly Arg Cys Lys 2065 2070 2075 2080 Pro Phe Ala Ala Ala Ala Asp Gly Thr Gly Trp Gly Glu Gly Val Gly 2085 2090 2095 Val Leu Leu Leu Glu Arg Leu Ser Asp Ala Arg Arg His Gly Arg Arg 2100 2105 2110 Val Leu Gly Val Val Arg Gly Ser Ala Val Asn Gln Asp Gly Ala Ser 2115 2120 2125 Asn Gly Leu Thr Ala Pro Asn Gly Pro Ser Gln Glu Arg Val Ile Arg 2130 2135 2140 Gln Ala Leu Ala Ser Gly Gly Leu Ser Ser Val Asp Val Asp Val Val 2145 2150 2155 2160 Glu Gly His Gly Thr Gly Thr Thr Leu Gly Asp Pro Ile Glu Ala Gln 2165 2170 2175 Ala Leu Leu Ala Thr Tyr Gly Gln Gly Arg Pro Val Asp Arg Pro Leu 2180 2185 2190 Trp Leu Gly Ser Val Lys Ser Asn Ile Gly His Thr Gln Ala Ala Ala 2195 2200 2205 Gly Val Ala Gly Val Ile Lys Met Val Met Ala Met Arg His Gly Val 2210 2215 2220 Val Pro Ala Ser Leu His Val Asp Val Pro Ser Pro His Val Glu Trp 2225 2230 2235 2240 Asp Ser Gly Ala Val Arg Leu Ala Val Glu Ser Val Pro Trp Pro Glu 2245 2250 2255 Val Glu Gly Arg Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Ala Ser 2260 2265 2270 Gly Thr Asn Ala His Val Ile Val Glu Ser Val Pro Asp Gly Leu Gly 2275 2280 2285 Glu Asp Ser Val Ser Val Ser Gly Glu Ala Pro Glu Thr Glu Thr Asp 2290 2295 2300 Gly Arg Leu Val Pro Trp Val Val Ser Ala Arg Ser Pro Gln Ala Leu 2305 2310 2315 2320 Arg Asp Gln Ala Leu Arg Leu Arg Asp Ala Val Ala Ala Asp Ser Thr 2325 2330 2335 Val Ser Val Gln Asp Val Gly Trp Ser Leu Leu Lys Thr Arg Ala Leu 2340 2345 2350 Phe Glu Gln Arg Ala Val Val Val Gly Arg Glu Arg Ala Glu Leu Leu 2355 2360 2365 Ser Gly Leu Ala Val Leu Ala Ala Gly Glu Glu His Pro Ala Val Thr 2370 2375 2380 Arg Ser Arg Glu Asp Gly Val Ala Ala Ser Gly Ala Val Val Trp Leu 2385 2390 2395 2400 Phe Ser Gly Gln Gly Ser Gln Leu Val Gly Met Gly Ala Gly Leu Tyr 2405 2410 2415 Glu Arg Phe Pro Val Phe Ala Ala Ala Phe Asp Glu Val Cys Gly Leu 2420 2425 2430 Leu Glu Gly Pro Leu Gly Val Glu Ala Gly Gly Leu Arg Glu Val Val 2435 2440 2445 Phe Arg Gly Pro Arg Glu Arg Leu Asp His Thr Met Trp Ala Gln Ala 2450 2455 2460 Gly Leu Phe Ala Leu Gln Val Gly Leu Ala Arg Leu Trp Glu Ser Val 2465 2470 2475 2480 Gly Val Arg Pro Asp Val Val Leu Gly His Ser Ile Gly Glu Ile Ala 2485 2490 2495 Ala Ala His Val Ala Gly Val Phe Asp Leu Ala Asp Ala Cys Arg Val 2500 2505 2510 Val Gly Ala Arg Ala Arg Leu Met Gly Gly Leu Pro Glu Gly Gly Ala 2515 2520 2525 Met Cys Ala Val Gln Ala Thr Pro Ala Glu Leu Ala Ala Asp Val Asp 2530 2535 2540 Asp Ser Gly Val Ser Val Ala Ala Val Asn Thr Pro Asp Ser Thr Val 2545 2550 2555 2560 Ile Ser Gly Pro Ser Gly Glu Val Asp Arg Ile Ala Gly Val Trp Arg 2565 2570 2575 Glu Arg Gly Arg Lys Thr Lys Ala Leu Ser Val Ser His Ala Phe His 2580 2585 2590 Ser Ala Leu Met Glu Pro Met Leu Ala Glu Phe Thr Glu Ala Ile Arg 2595 2600 2605 Glu Val Lys Phe Thr Arg Pro Lys Val Ser Leu Ile Ser Asn Val Ser 2610 2615 2620 Gly Leu Glu Ala Gly Glu Glu Ile Ala Ser Pro Glu Tyr Trp Ala Arg 2625 2630 2635 2640 His Val Arg Gln Thr Val Leu Phe Gln Pro Gly Ile Ala Gln Val Ala 2645 2650 2655 Ser Thr Ala Gly Val Phe Val Glu Leu Gly Pro Gly Pro Val Leu Thr 2660 2665 2670 Thr Ala Ala Gln His Thr Leu Asp Asp Val Thr Asp Arg His Gly Pro 2675 2680 2685 Glu Pro Val Leu Val Ser Ser Leu Ala Gly Glu Arg Pro Glu Glu Ser 2690 2695 2700 Ala Phe Val Glu Ala Met Ala Arg Leu His Thr Ala Gly Val Ala Val 2705 2710 2715 2720 Asp Trp Ser Val Leu Phe Ala Gly Asp Arg Val Pro Gly Leu Val Glu 2725 2730 2735 Leu Pro Thr Tyr Ala Phe Gln Arg Glu Arg Phe Trp Leu Ser Gly Arg 2740 2745 2750 Ser Gly Gly Gly Asp Ala Ala Thr Leu Gly Leu Val Ala Ala Gly His 2755 2760 2765 Pro Leu Leu Gly Ala Ala Val Glu Phe Ala Asp Arg Gly Gly Cys Leu 2770 2775 2780 Leu Thr Gly Arg Leu Ser Arg Ser Gly Val Ser Trp Leu Ala Asp His 2785 2790 2795 2800 Val Val Ala Gly Ala Val Leu Val Pro Gly Ala Ala Leu Val Glu Trp 2805 2810 2815 Ala Leu Arg Ala Gly Asp Glu Val Gly Cys Val Thr Val Glu Glu Leu 2820 2825 2830 Met Leu Gln Ala Pro Leu Val Val Pro Glu Ala Ser Gly Leu Arg Val 2835 2840 2845 Gln Val Val Val Glu Glu Ala Gly Glu Asp Gly Arg Arg Gly Val Gln 2850 2855 2860 Ile Tyr Ser Arg Pro Asp Ala Asp Ala Val Ser Gly Asp Asp Ser Trp 2865 2870 2875 2880 Ile Cys His Ala Thr Gly Thr Leu Thr Pro Gln His Thr Asp Ala Pro 2885 2890 2895 Asn Asp Gly Leu Ala Gly Ala Trp Pro Ala Ala Gly Ala Val Pro Val 2900 2905 2910 Asp Leu Ala Gly Phe Tyr Glu Arg Val Ala Asp Ala Gly Tyr Ala Tyr 2915 2920 2925 Gly Pro Gly Phe Gln Gly Leu Arg Ala Val Trp Arg His Gly Gln Asp 2930 2935 2940 Leu Leu Ala Glu Val Val Leu Pro Glu Ala Ala Gly Ala His Asp Gly 2945 2950 2955 2960 Tyr Gly Ile His Pro Ala Leu Leu Asp Ala Thr Leu His Pro Ala Leu 2965 2970 2975 Leu Leu Asp Trp Pro Gly Glu Val Gln Asp Asp Asp Gly Lys Val Trp 2980 2985 2990 Leu Pro Phe Thr Trp Asn Gln Val Ser Leu Arg Ala Ala Gly Ala Ala 2995 3000 3005 Thr Val Arg Val Arg Leu Ser Pro Gly Glu His Asp Glu Ala Glu Arg 3010 3015 3020 Glu Val Gln Val Leu Val Ala Asp Ala Thr Gly Thr Asp Val Leu Ser 3025 3030 3035 3040 Val Gly Ser Val Thr Leu Arg Pro Ala Asp Ile Arg Gln Leu Gln Ala 3045 3050 3055 Val Pro Gly His Asp Asp Gly Leu Phe Ser Val Asp Trp Thr Pro Leu 3060 3065 3070 Pro Leu Ser Arg Thr Asp Val Ser Gln Thr Asp Ala Asp Gly Asp Ala 3075 3080 3085 Asp Trp Val Val Leu Ser Asp Gly Val Gly Ser Leu Ala Asp Val Val 3090 3095 3100 Ser Ala Ala Gly Gly Glu Ala Pro Trp Ala Val Val Ala Pro Val Gly 3105 3110 3115 3120 Ala Ser Ala Gly Gly Gly Leu Ala Gly Phe Asp Arg Arg Glu Gly Leu 3125 3130 3135 Asp Gly Arg Leu Val Val Glu Arg Val Leu Ser Leu Val Gln Glu Phe 3140 3145 3150 Leu Ala Ala Pro Glu Leu Ala Glu Ser Arg Leu Leu Val Leu Thr Arg 3155 3160 3165 Gly Ala Val Ala Thr Gly Gly Asp Gly Asp Gly Asp Val Asp Ala Ser 3170 3175 3180 Ala Ala Ala Val Trp Gly Leu Val Arg Ser Ala Gln Ser Glu Asn Pro 3185 3190 3195 3200 Gly Arg Phe Ile Leu Leu Asp Val Asp Met Asp Val Asp Val Asp Val 3205 3210 3215 Asp Met Asp Val Asp Val Asp Val Asp Val Asp Val Asp Val Asp Gly 3220 3225 3230 Asp Gly Asn Gly Ser Asp Leu Asp Pro Asp Leu Asn Gly Arg Arg Leu 3235 3240 3245 Pro His Ala Thr Leu Arg His Ala Ala Glu Glu Leu Asp Glu Pro Gln 3250 3255 3260 Leu Ala Leu Arg Asp Gly Gln Leu Leu Val Pro Arg Leu Val Arg Ala 3265 3270 3275 3280 Thr Gly Gly Gly Leu Val Val Ala Pro Thr Asp Arg Ala Trp Arg Leu 3285 3290 3295 Asp Lys Gly Ser Ala Glu Thr Leu Glu Ser Val Ala Pro Val Ala Tyr 3300 3305 3310 Pro Gly Val Met Glu Pro Leu Gly Pro Gly Gln Val Arg Leu Gly Ile 3315 3320 3325 His Ala Ala Gly Ile Asn Phe Arg Asp Val Leu Val Ser Leu Gly Met 3330 3335 3340 Val Pro Gly Gln Val Gly Leu Gly Gly Glu Gly Ala Gly Val Val Thr 3345 3350 3355 3360 Glu Thr Gly Pro Asp Val Thr His Leu Ser Val Gly Asp Arg Val Met 3365 3370 3375 Gly Val Leu His Gly Ser Phe Gly Pro Thr Ala Val Ala Asp Thr Arg 3380 3385 3390 Met Val Ala Pro Val Pro Gln Gly Trp Asp Met Arg Gln Ala Ala Ala 3395 3400 3405 Met Pro Val Ala Tyr Leu Thr Ala Trp Tyr Gly Leu Val Glu Leu Ala 3410 3415 3420 Gly Leu Lys Ala Gly Glu Arg Val Leu Ile His Ala Ala Thr Gly Gly 3425 3430 3435 3440 Val Gly Met Ala Ala Val Gln Ile Ala Arg His Leu Gly Ala Glu Val 3445 3450 3455 Phe Ala Thr Ala Ser Ala Ala Lys His Val Val Leu Glu Glu Met Gly 3460 3465 3470 Ile Asp Ala Ala His Arg Ala Ser Ser Arg Asp Leu Ala Phe Glu Asp 3475 3480 3485 Thr Phe Arg Gln Ala Thr Asp Gly Arg Gly Met Asp Val Val Leu Asn 3490 3495 3500 Ser Leu Thr Gly Glu Phe Ile Asp Ala Ser Leu Arg Leu Leu Gly Asp 3505 3510 3515 3520 Gly Gly Arg Phe Leu Glu Met Gly Lys Thr Asp Val Arg Thr Pro Glu 3525 3530 3535 Glu Val Ala Ala Glu Tyr Pro Gly Val Thr Tyr Thr Val Tyr Asp Leu 3540 3545 3550 Val Thr Asp Ala Gly Pro Asp Arg Ile Ala Val Met Met Ser Glu Leu 3555 3560 3565 Gly Glu Arg Phe Ala Ser Gly Ala Leu Asp Pro Leu Pro Val Arg Ser 3570 3575 3580 Trp Pro Leu Asp Lys Ala Arg Glu Ala Phe Arg Phe Met Ser Gln Ala 3585 3590 3595 3600 Lys His Thr Gly Lys Leu Val Leu Asp Val Pro Ala Pro Leu Asp Pro 3605 3610 3615 Asp Gly Thr Val Leu Ile Thr Gly Gly Thr Gly Ala Leu Gly Gln Val 3620 3625 3630 Val Ala Glu His Leu Val Arg Glu Trp Gly Val Arg His Leu Leu Leu 3635 3640 3645 Ala Ser Arg Arg Gly Leu Asp Ala Pro Gly Ser Gly Glu Leu Ala Asp 3650 3655 3660 Arg Leu Ser Asp Leu Gly Ala Glu Val Thr Val Ala Ala Ala Asp Val 3665 3670 3675 3680 Ser Asp Pro Ala Ser Val Val Glu Leu Val Gly Lys Thr Asp Pro Ser 3685 3690 3695 His Pro Leu Thr Gly Val Val His Ala Ala Gly Val Leu Glu Asp Gly 3700 3705 3710 Ile Val Thr Ala Gln Thr Pro Glu Gly Leu Ala Arg Val Trp Ala Ala 3715 3720 3725 Lys Ala Ala Ala Ala Ala Asn Leu His Glu Ala Thr Arg Glu Met Arg 3730 3735 3740 Leu Gly Leu Phe Val Val Phe Ser Ser Ala Ala Ala Thr Leu Gly Ser 3745 3750 3755 3760 Pro Gly Gln Ala Asn Tyr Ala Ala Ala Asn Ala Tyr Cys Asp Ala Leu 3765 3770 3775 Met Gln Arg Arg Arg Ala Ala Gly Gln Val Gly Leu Ser Val Gly Trp 3780 3785 3790 Gly Leu Trp Glu Ala Pro Asp Ala Lys Pro Gly Val Ala Ala Asp Ala 3795 3800 3805 Lys Pro Asp Val Ala Ala Asp Ala Lys Thr Gly Val Ala Ala Asp Gly 3810 3815 3820 Thr Pro Gln Gly Met Thr Gly Thr Leu Ser Gly Thr Asp Val Ala Arg 3825 3830 3835 3840 Met Ala Arg Ile Gly Val Lys Ala Met Thr Ser Ala His Gly Leu Ala 3845 3850 3855 Leu Leu Asp Ala Ala His Arg His Gly Arg Pro His Leu Val Ala Val 3860 3865 3870 Asp Leu Asp Thr Arg Val Leu Ala His Lys Pro Ala Pro Ala Leu Pro 3875 3880 3885 Ala Leu Leu Arg Ala Phe Ala Gly Asp Gln Gly Gly Gln Gly Gly Gly 3890 3895 3900 Arg Gly Gly Gly Arg Gly Gly Gly Pro Ala Arg Pro Ala Ala Ala Thr 3905 3910 3915 3920 Thr Arg Gln Asn Val Asp Trp Ala Ala Lys Leu Ser Val Leu Thr Ala 3925 3930 3935 Glu Glu Gln His Arg Thr Leu Leu Asp Leu Val Arg Thr His Ala Ala 3940 3945 3950 Ala Val Leu Gly His Ala Gly Thr Asp Ala Val Arg Ala Asp Ala Ala 3955 3960 3965 Phe Gln Asp Leu Gly Phe Asp Ser Leu Thr Ala Val Glu Leu Arg Asn 3970 3975 3980 Arg Leu Ser Ala Ser Thr Gly Leu Arg Leu Pro Ala Thr Phe Ile Phe 3985 3990 3995 4000 Arg His Pro Thr Pro Ser Ala Ile Ala Asp Glu Leu Arg Ala Gln Leu 4005 4010 4015 Ala Pro Ala Gly Ala Asp Pro Ala Ala Pro Leu Phe Gly Glu Leu Asp 4020 4025 4030 Lys Leu Glu Thr Val Ile Thr Gly His Ala His Asp Glu Ser Thr Arg 4035 4040 4045 Thr Arg Leu Ala Ala Arg Leu Gln Asn Leu Leu Trp Arg Leu Asp Asp 4050 4055 4060 Thr Ser Ala Arg Ser Asp His Ala Ala Gly Ala Ser Asp Ala Asp Gly 4065 4070 4075 4080 Asp Ala Val Glu Asn Arg Asp Leu Glu Ser Ala Ser Asp Asp Glu Leu 4085 4090 4095 Phe Glu Leu Ile Asp Arg Glu Leu Pro Ser 4100 4105 24 1700 PRT Streptomyces cinnamonensis 24 Met Pro Gly Thr Asn Asp Met Pro Gly Thr Glu Asp Lys Leu Arg His 1 5 10 15 Tyr Leu Lys Arg Val Thr Ala Asp Leu Gly Gln Thr Arg Gln Arg Leu 20 25 30 Arg Asp Val Glu Glu Arg Gln Arg Glu Pro Ile Ala Ile Val Ala Met 35 40 45 Ala Cys Arg Tyr Pro Gly Gly Val Ala Ser Pro Glu Gln Leu Trp Asp 50 55 60 Leu Val Ala Ser Arg Gly Asp Ala Ile Glu Glu Phe Pro Ala Asp Arg 65 70 75 80 Gly Trp Asp Val Ala Gly Leu Tyr His Pro Asp Pro Asp His Pro Gly 85 90 95 Thr Thr Tyr Val Arg Glu Ala Gly Phe Leu Arg Asp Ala Ala Arg Phe 100 105 110 Asp Ala Asp Phe Phe Gly Ile Asn Pro Arg Glu Ala Leu Ala Ala Asp 115 120 125 Pro Gln Gln Arg Val Leu Leu Glu Val Ser Trp Glu Leu Phe Glu Arg 130 135 140 Ala Gly Ile Asp Pro Ala Thr Leu Lys Asp Thr Leu Thr Gly Val Tyr 145 150 155 160 Ala Gly Val Ser Ser Gln Asp His Met Ser Gly Ser Arg Val Pro Pro 165 170 175 Glu Val Glu Gly Tyr Ala Thr Thr Gly Thr Leu Ser Ser Val Ile Ser 180 185 190 Gly Arg Ile Ala Tyr Thr Phe Gly Leu Glu Gly Pro Ala Val Thr Leu 195 200 205 Asp Thr Ala Cys Ser Ala Ser Leu Val Ala Ile His Leu Ala Cys Gln 210 215 220 Ala Leu Arg Gln Gly Asp Cys Gly Leu Ala Val Ala Gly Gly Val Thr 225 230 235 240 Val Leu Ser Thr Pro Thr Ala Phe Val Glu Phe Ser Arg Gln Arg Gly 245 250 255 Leu Ala Pro Asp Gly Arg Cys Lys Pro Phe Ala Glu Ala Ala Asp Gly 260 265 270 Thr Gly Phe Ser Glu Gly Val Gly Leu Ile Leu Leu Glu Arg Leu Ser 275 280 285 Asp Ala Arg Arg Asn Gly His Gln Val Leu Gly Val Val Arg Gly Ser 290 295 300 Ala Val Asn Gln Asp Gly Ala Ser Asn Gly Leu Thr Ala Pro Asn Asp 305 310 315 320 Val Ala Gln Glu Arg Val Ile Arg Gln Ala Leu Thr Asn Ala Arg Val 325 330 335 Thr Pro Asp Ala Val Asp Ala Val Glu Ala His Gly Thr Gly Thr Thr 340 345 350 Leu Gly Asp Pro Ile Glu Gly Asn Ala Leu Leu Ala Thr Tyr Gly Lys 355 360 365 Asp Arg Pro Ala Asp Arg Pro Leu Trp Leu Gly Ser Val Lys Ser Asn 370 375 380 Ile Gly His Thr Gln Ala Ala Ala Gly Val Ala Gly Val Ile Lys Met 385 390 395 400 Val Met Ala Met Arg His Gly Glu Leu Pro Ala Ser Leu His Ile Asp 405 410 415 Arg Pro Thr Pro His Val Asp Trp Glu Gly Gly Gly Val Arg Leu Leu 420 425 430 Thr Asp Pro Val Pro Trp Pro Arg Ala Asp Arg Pro Arg Arg Ala Gly 435 440 445 Val Ser Ser Phe Gly Ile Ser Gly Thr Asn Ala His Leu Ile Val Glu 450 455 460 Gln Ala Pro Ala Pro Pro Asp Thr Ala Asp Asp Ala Pro Glu Gly Ala 465 470 475 480 Ala Thr Pro Gly Ala Ser Asp Gly Leu Val Val Pro Trp Val Val Ser 485 490 495 Ala Arg Ser Pro Gln Ala Leu Arg Asp Gln Ala Leu Arg Leu Arg Asp 500 505 510 Phe Ala Gly Asp Ala Ser Arg Ala Pro Leu Thr Asp Val Gly Trp Ser 515 520 525 Leu Leu Arg Ser Arg Ala Leu Phe Glu Gln Arg Ala Val Val Ala Gly 530 535 540 Arg Glu Arg Ala Glu Leu Leu Ala Gly Leu Ala Ala Leu Ala Ala Gly 545 550 555 560 Glu Glu His Pro Ala Val Thr Arg Ser Arg Glu Glu Ala Ala Val Ala 565 570 575 Ala Ser Gly Asp Val Val Trp Leu Phe Ser Gly Gln Gly Ser Gln Leu 580 585 590 Val Gly Met Gly Ala Gly Leu Tyr Glu Arg Phe Pro Val Phe Ala Ala 595 600 605 Ala Phe Asp Glu Val Cys Gly Leu Leu Glu Gly Glu Leu Gly Val Gly 610 615 620 Ser Gly Gly Leu Arg Glu Val Val Phe Trp Gly Pro Arg Glu Arg Leu 625 630 635 640 Asp His Thr Val Trp Ala Gln Ala Gly Leu Phe Ala Leu Gln Val Gly 645 650 655 Leu Ala Arg Leu Trp Glu Ser Val Gly Val Arg Pro Asp Val Val Leu 660 665 670 Gly His Ser Ile Gly Glu Ile Ala Ala Ala His Val Ala Gly Val Phe 675 680 685 Asp Leu Ala Asp Ala Cys Arg Val Val Gly Ala Arg Ala Arg Leu Met 690 695 700 Gly Gly Leu Pro Glu Gly Gly Ala Met Cys Ala Val Gln Ala Thr Pro 705 710 715 720 Ala Glu Leu Ala Ala Asp Val Asp Gly Ser Ser Val Ser Val Ala Ala 725 730 735 Val Asn Thr Pro Asp Ser Thr Val Ile Ser Gly Pro Ser Gly Glu Val 740 745 750 Asp Arg Ile Ala Gly Val Trp Arg Glu Arg Gly Arg Lys Thr Lys Ala 755 760 765 Leu Ser Val Ser His Ala Phe His Ser Ala Leu Met Glu Pro Met Leu 770 775 780 Gly Glu Phe Thr Glu Ala Ile Arg Gly Val Lys Phe Arg Gln Pro Ser 785 790 795 800 Ile Pro Leu Met Ser Asn Val Ser Gly Glu Arg Ala Gly Glu Glu Ile 805 810 815 Thr Ser Pro Glu Tyr Trp Ala Arg His Val Arg Gln Thr Val Leu Phe 820 825 830 Gln Pro Gly Val Ala Gln Val Ala Ala Glu Ala Arg Ala Phe Val Glu 835 840 845 Leu Gly Pro Gly Pro Val Leu Thr Ala Ala Ala Gln His Thr Leu Asp 850 855 860 His Ile Thr Glu Pro Glu Gly Pro Glu Pro Val Val Thr Ala Ser Leu 865 870 875 880 His Pro Asp Arg Pro Asp Asp Val Ala Phe Ala His Ala Met Ala Asp 885 890 895 Leu His Val Ala Gly Ile Ser Val Asp Trp Ser Ala Tyr Phe Pro Asp 900 905 910 Asp Pro Ala Pro Arg Thr Val Asp Leu Pro Thr Tyr Ala Phe Gln Gly 915 920 925 Arg Arg Phe Trp Leu Ala Asp Ile Ala Ala Pro Glu Ala Val Ser Ser 930 935 940 Thr Asp Gly Glu Glu Ala Gly Phe Trp Ala Ala Val Glu Gly Ala Asp 945 950 955 960 Phe Gln Ala Leu Cys Asp Thr Leu His Leu Lys Asp Asp Glu His Arg 965 970 975 Ala Ala Leu Glu Thr Val Phe Pro Ala Leu Ser Ala Trp Arg Arg Glu 980 985 990 Arg Arg Glu Arg Ser Ile Val Asp Ala Trp Arg Tyr Arg Val Asp Trp 995 1000 1005 Arg Arg Val Glu Leu Pro Thr Pro Val Pro Gly Ala Gly Thr Gly Pro 1010 1015 1020 Asp Ala Asp Thr Gly Leu Gly Ala Trp Leu Ile Val Ala Pro Thr His 1025 1030 1035 1040 Gly Ser Gly Thr Trp Pro Gln Ala Cys Ala Arg Ala Leu Glu Glu Ala 1045 1050 1055 Gly Ala Pro Val Arg Ile Val Glu Ala Gly Pro His Ala Asp Arg Ala 1060 1065 1070 Asp Met Ala Asp Leu Val Gln Ala Trp Arg Ala Ser Cys Ala Asp Asp 1075 1080 1085 Thr Thr Gln Leu Gly Gly Val Leu Ser Leu Leu Ala Leu Ala Glu Ala 1090 1095 1100 Pro Ala Thr Ser Ser Asp Thr Thr Ser His Thr Ser Thr Ser Cys Gly 1105 1110 1115 1120 Thr Gly Ser Leu Ala Ser His Gly Leu Thr Gly Thr Leu Thr Leu Leu 1125 1130 1135 His Gly Leu Leu Asp Ala Gly Val Glu Ala Pro Leu Trp Cys Ala Thr 1140 1145 1150 Arg Gly Ala Val Ser Cys Gly Asp Ala Asp Pro Leu Val Ser Pro Ser 1155 1160 1165 Gln Ala Pro Val Trp Gly Leu Gly Arg Val Ala Ala Leu Glu His Pro 1170 1175 1180 Glu Leu Trp Gly Gly Leu Val Asp Leu Pro Ala Asp Pro Glu Ser Leu 1185 1190 1195 1200 Asp Ala Ser Ala Leu Tyr Ala Val Leu Arg Gly Asp Gly Gly Glu Asp 1205 1210 1215 Gln Val Ala Leu Arg Arg Gly Ala Val Leu Gly Arg Arg Leu Val Pro 1220 1225 1230 Asp Ala Thr Pro Asp Val Ala Pro Gly Ser Ser Pro Asp Val Ser Gly 1235 1240 1245 Gly Ala Ala His Ala Asp Ala Thr Ser Gly Glu Trp Gln Pro His Gly 1250 1255 1260 Ala Val Leu Val Thr Gly Gly Val Gly His Leu Ala Asp Gln Val Val 1265 1270 1275 1280 Arg Trp Leu Ala Ala Ser Gly Ala Glu His Val Val Leu Leu Asp Thr 1285 1290 1295 Gly Pro Ala Asn Ser Arg Gly Pro Gly Arg Asn Asp Asp Leu Ala Ala 1300 1305 1310 Glu Ala Ala Glu His Gly Thr Glu Leu Thr Val Leu Arg Ser Leu Ser 1315 1320 1325 Glu Leu Thr Asp Val Ser Val Arg Pro Ile Arg Thr Val Ile His Thr 1330 1335 1340 Ser Leu Pro Gly Glu Leu Ala Pro Leu Ala Glu Val Thr Pro Asp Ala 1345 1350 1355 1360 Leu Gly Ala Ala Val Ser Ala Ala Ala Arg Leu Ser Glu Leu Pro Gly 1365 1370 1375 Ile Gly Ser Val Glu Thr Val Leu Phe Phe Ser Ser Val Thr Ala Ser 1380 1385 1390 Leu Gly Ser Arg Glu His Gly Ala Tyr Ala Ala Ala Asn Ala Tyr Leu 1395 1400 1405 Asp Ala Leu Ala Gln Arg Ala Gly Ala Asp Ala Ala Ser Pro Arg Thr 1410 1415 1420 Val Ser Val Gly Trp Gly Ile Trp Asp Leu Pro Asp Asp Gly Asp Val 1425 1430 1435 1440 Ala Arg Gly Ala Ala Gly Leu Ser Arg Arg Gln Gly Leu Pro Pro Leu 1445 1450 1455 Glu Pro Gln Leu Ala Leu Gly Ala Leu Arg Ala Ala Leu Asp Gly Gly 1460 1465 1470 Lys Gly His Thr Leu Val Ala Asp Ile Glu Trp Glu Arg Phe Ala Pro 1475 1480 1485 Leu Phe Thr Leu Ala Arg Pro Thr Arg Leu Leu Asp Gly Ile Pro Ala 1490 1495 1500 Ala Gln Arg Val Leu Asp Ala Ser Ser Glu Ser Ala Glu Ala Ser Glu 1505 1510 1515 1520 Asn Ala Ser Ala Leu Arg Arg Glu Leu Thr Ala Leu Pro Val Arg Glu 1525 1530 1535 Arg Thr Gly Ala Leu Leu Asp Leu Val Arg Lys Gln Val Ala Ala Val 1540 1545 1550 Leu Arg Tyr Glu Pro Gly Gln Asp Val Ala Pro Glu Lys Ala Phe Lys 1555 1560 1565 Asp Leu Gly Phe Asp Ser Leu Val Val Val Glu Leu Arg Asn Arg Leu 1570 1575 1580 Arg Ala Ala Thr Gly Leu Arg Leu Pro Ala Thr Leu Val Tyr Asp Tyr 1585 1590 1595 1600 Pro Thr Pro Arg Thr Leu Ala Ala His Leu Leu Asp Arg Val Leu Pro 1605 1610 1615 Asp Gly Gly Ala Ala Glu Leu Pro Val Ala Ala His Leu Asp Asp Leu 1620 1625 1630 Glu Ala Ala Leu Thr Asp Leu Pro Ala Asp Asp Pro Arg Arg Lys Gly 1635 1640 1645 Leu Val Arg Arg Leu Gln Thr Leu Leu Trp Lys Gln Pro Asp Ala Met 1650 1655 1660 Gly Ala Ala Gly Pro Ala Asp Glu Glu Glu Gln Ala Ala Pro Glu Asp 1665 1670 1675 1680 Leu Ser Thr Ala Ser Ala Asp Asp Met Phe Ala Leu Ile Asp Arg Glu 1685 1690 1695 Trp Gly Thr Arg 1700 25 980 PRT Streptomyces cinnamonensis 25 Val Ser Gly Val Glu Arg Gly Val Gly Ser Ala Gly Pro Val Glu Gln 1 5 10 15 Gly Asp Gly Leu Ala Gly Leu Val Glu Arg Ala Glu Ala Leu Ala Ala 20 25 30 Leu Arg Gly Ala Phe Asp Gly Ser Pro Gly Thr Gly Gly Ser Leu Val 35 40 45 Val Leu Ser Gly Ala Val Gly Thr Gly Lys Thr Ala Leu Leu Arg Ala 50 55 60 Trp Ala Asp Arg Ile Gly Ala Asp Ala Asp Ala Leu Val Leu Thr Ala 65 70 75 80 Thr Ala Cys Arg Ala Glu Arg Asp Leu Pro Leu Gly Val Leu Glu Gln 85 90 95 Leu Val Arg Ser Pro Gly Leu Pro Pro Ala Ser Ala Glu Arg Ala Leu 100 105 110 Ala Trp Trp Asp Glu Glu Ala Ser Ala Thr Pro Gly Lys Thr Asp Ala 115 120 125 Asn Gly Thr Ser Ala Asn Gly Thr Asp Ala Asn Gly Thr Gly Ala Gly 130 135 140 Gln Thr Gly Ala Gly Gln Ala Gly Val Gly Gln Thr Gly Val Gly Gly 145 150 155 160 Glu Pro Val Leu Ala Ala Ser Ala Leu Arg Gly Leu Cys Glu Val Leu 165 170 175 Arg Asp Leu Leu Ala Glu Arg Pro Val Val Val Ala Val Asp Asp Ala 180 185 190 His His Ala Asp Ala Ala Ser Leu Gln Cys Leu Leu Ser Val Val Arg 195 200 205 Arg Leu Arg Ser Ala Arg Leu His Val Leu Phe Thr Glu Tyr Ala His 210 215 220 Gln Lys Ala Gln Asn Ala Leu Leu Ser Ser Glu Phe Leu His Glu Pro 225 230 235 240 Ala Leu Arg Arg Ile Arg Leu Glu Pro Leu Ser Lys Ala Gly Val Glu 245 250 255 Ala Leu Leu Ala Arg His Leu Asp Glu Arg Thr Ala Gln Asp Leu Thr 260 265 270 Pro Val Val His Gly Met Ser Ala Gly His Pro Leu Leu Val Arg Ala 275 280 285 Leu Ala Glu Asp His Arg Ala Ala Gly Gly Ala Gly Glu Ala Tyr Gly 290 295 300 Arg Ala Val Leu Ser Phe Leu Tyr Arg His Glu Thr Pro Val Thr Gln 305 310 315 320 Val Ala Arg Ala Ile Ala Ala Leu Gly Ala His Ala Gly Pro Gly Gln 325 330 335 Val Gly Arg Leu Leu Asp Val Asp Ala Ala Ser Val Glu Arg Ala Val 340 345 350 Arg Gln Leu Thr Val Ala Glu Val Leu His Glu Gly Arg Leu Cys His 355 360 365 Pro Ala Phe Ala Ala Ala Val Leu Asp Gly Met Pro Pro Glu Glu Arg 370 375 380 Arg Ala Leu His Gly Arg Val Ala Asp Leu Leu His Glu Glu Gly Ala 385 390 395 400 Pro Ala Thr Glu Val Ala Ala His Leu Val Ala Ala Asp Arg Ser Asp 405 410 415 Ala Pro Trp Ala Val Pro Val Phe Gln Glu Ala Ala Gln Leu Ala Leu 420 425 430 Asp Glu Asp Gln Val Glu Thr Gly Val Asp Tyr Leu Arg Ala Ala His 435 440 445 Gln Arg Cys Arg Gly Ala Ala Gln Arg Ala Ala Val Val Gly Ala Leu 450 455 460 Ala Asp Ala Glu Trp Arg Leu Asp Pro Ala Lys Val Leu Arg His Leu 465 470 475 480 Pro Asp Pro Ala Ala Met Ala Pro Gln Thr Asp Pro Ala Ala Leu Ala 485 490 495 Pro His Thr Asp Pro Ala Pro Thr Ala Ala Pro Thr Ala Ala Pro Thr 500 505 510 Pro Thr Pro Ile Pro Thr Thr Pro Pro Leu Pro Thr His Leu Leu Trp 515 520 525 His Gly Arg Val Glu Glu Gly Leu Asp Ala Ile Gly Thr Leu Thr Gly 530 535 540 Pro Gly Pro Asn Pro Ala Gly Ala Pro Pro Met Asn Pro Ala Asp Leu 545 550 555 560 Asp Thr Pro Trp Leu Trp Gly Ala Tyr Leu Tyr Pro Gly His Val Lys 565 570 575 Glu Arg Leu Gly Ser Gly Ala Leu Ser Pro Gln Arg Ser Thr Pro Pro 580 585 590 Ala Val Thr Pro Glu Leu Gln Gly Ala Gly Thr Leu Met Asn Asp Leu 595 600 605 Leu His Gly Gly Glu Arg Asp Ala Thr Glu Ala Ala Glu Arg Ala Leu 610 615 620 Asn Arg Tyr Arg Leu Gly Pro Arg Thr Ile Ala Val Gln Thr Ala Ala 625 630 635 640 Leu Ala Ala Leu Thr Tyr Arg Asp Arg Pro His Arg Ala Ala Ala Trp 645 650 655 Cys Asp Gly Leu Val Ala Gln Ala Asp Glu Arg Asn Ser Pro Thr Trp 660 665 670 Arg Ala Leu Phe Thr Ala Trp Arg Ala Leu Leu His Leu Arg Gln Gly 675 680 685 Asp Pro Ala Ala Ala Glu Gln Arg Ala Glu Thr Ala Leu Ala Leu Leu 690 695 700 Gly Ser Lys Gly Trp Gly Ala Ala Ile Gly Leu Pro Leu Ala Ala Ala 705 710 715 720 Val Gln Ala Lys Ala Ala Leu Gly Asp Val Asp Gly Ala Ala Ala Leu 725 730 735 Leu Glu Arg Pro Val Pro Gln Ala Val Phe Gln Thr Arg Thr Gly Leu 740 745 750 His Tyr Leu Ala Ala Arg Gly Arg Tyr His Leu Ala Thr Gly Cys His 755 760 765 Tyr Ala Ala Leu Cys Asp Phe Tyr Ala Cys Gly Thr Arg Met Ser Ser 770 775 780 Trp Gly Val Asp Leu Pro Ala Leu Glu Pro Trp Arg Leu Gly Ala Ala 785 790 795 800 Glu Ala Tyr Leu Ala Leu Gly Glu Gly Leu Leu Ala Arg Gln Leu Val 805 810 815 Asp Gly Gln Leu Pro Leu Pro Thr Pro Asp Asp Gly Arg Thr Trp Gly 820 825 830 Met Thr Leu Arg Leu Arg Ala Ala Thr Ser Pro Ala Pro Ala Arg Ala 835 840 845 Glu Leu Leu Asp Glu Ala Val Ala Val Leu Arg Glu Ser Gly Asp Thr 850 855 860 Phe Glu Leu Ala Arg Ala Val Ala Asp Gln Ala Val Ala Val Arg Glu 865 870 875 880 Gly Gly Glu Ala Glu Arg Ala Arg Leu Leu Ala Arg Lys Ala Glu Leu 885 890 895 Leu Ala Arg Arg Trp Gly Ser Ala Pro Ala Pro Ala Thr Val Pro Glu 900 905 910 Pro Pro Glu Arg Pro Gly Pro Ala Thr Pro Asp Ala Glu Leu Thr Ser 915 920 925 Ala Glu Arg Arg Val Ala Glu Leu Ala Ala Glu Gly Phe Thr Asn Arg 930 935 940 Glu Ile Ser Arg Lys Leu Cys Val Thr Val Ser Thr Val Glu Gln His 945 950 955 960 Leu Thr Arg Ile Tyr Arg Lys Leu Asp Val Arg Arg Leu Asp Leu Gln 965 970 975 Ala Ala Leu Gly 980 26 496 PRT Streptomyces cinnamonensis 26 Val Thr Thr Thr Arg Pro Ala His Ala Val Val Leu Gly Ala Ser Met 1 5 10 15 Ala Gly Thr Leu Ala Ala His Val Leu Ala Arg His Val Asp Ala Val 20 25 30 Thr Val Val Glu Arg Asp Ala Leu Pro Glu Glu Pro Gln His Arg Lys 35 40 45 Gly Val Pro Gln Ala Arg His Ala His Leu Leu Trp Ser Asn Gly Ala 50 55 60 Arg Leu Ile Glu Glu Met Leu Pro Gly Thr Thr Asp Arg Leu Leu Ala 65 70 75 80 Ala Gly Ala Arg Arg Leu Gly Phe Pro Glu Asp Leu Val Thr Leu Thr 85 90 95 Gly Gln Gly Trp Gln His Arg Phe Pro Ala Thr Gln Phe Ala Leu Val 100 105 110 Ala Ser Arg Pro Leu Leu Asp Leu Thr Val Arg Gln Gln Ala Leu Gly 115 120 125 Ala Asp Asn Ile Thr Val Arg Gln Arg Thr Glu Ala Val Glu Leu Thr 130 135 140 Gly Ser Gly Gly Gly Ser Gly Gly Arg Val Thr Gly Val Val Val Arg 145 150 155 160 Asp Leu Asp Ser Gly Arg Gln Glu Gln Leu Glu Ala Asp Leu Val Ile 165 170 175 Asp Ala Thr Gly Arg Gly Ser Arg Leu Lys Gln Trp Leu Ala Ala Leu 180 185 190 Gly Val Pro Ala Leu Glu Glu Asp Val Val Asp Ala Gly Val Ala Tyr 195 200 205 Ala Thr Arg Leu Phe Lys Ala Pro Pro Gly Ala Thr Thr His Phe Pro 210 215 220 Ala Val Asn Ile Ala Ala Asp Asp Arg Val Arg Glu Pro Gly Arg Phe 225 230 235 240 Gly Val Val Tyr Pro Ile Glu Gly Gly Arg Trp Leu Ala Thr Leu Ser 245 250 255 Cys Thr Arg Gly Ala Gln Leu Pro Thr His Glu Asp Glu Phe Ile Pro 260 265 270 Phe Ala Glu Asn Leu Asn His Pro Ile Leu Ala Asp Leu Leu Arg Asp 275 280 285 Ala Glu Pro Leu Thr Pro Val Phe Gly Ser Arg Ser Gly Ala Asn Arg 290 295 300 Arg Leu Tyr Pro Glu Arg Leu Glu Gln Trp Pro Asp Gly Leu Leu Val 305 310 315 320 Ile Gly Asp Ser Leu Thr Ala Phe Asn Pro Ile Tyr Gly His Gly Met 325 330 335 Ser Ser Ala Ala Arg Cys Ala Thr Thr Ile Asp Arg Glu Phe Glu Arg 340 345 350 Ser Val Gln Glu Gly Thr Gly Ser Ala Arg Ala Gly Thr Arg Ala Leu 355 360 365 Gln Lys Ala Ile Gly Ala Ala Val Asp Asp Pro Trp Ile Leu Ala Ala 370 375 380 Thr Lys Asp Ile Asp Tyr Val Asn Cys Arg Val Ser Ala Thr Asp Pro 385 390 395 400 Arg Leu Ile Gly Val Asp Thr Glu Gln Arg Leu Arg Phe Ala Glu Ala 405 410 415 Ile Thr Ala Ala Ser Ile Arg Ser Pro Lys Ala Ser Glu Ile Val Thr 420 425 430 Asp Val Met Ser Leu Asn Ala Pro Gln Ala Glu Leu Gly Ser Asn Arg 435 440 445 Phe Leu Met Ala Met Arg Ala Asp Glu Arg Leu Pro Glu Leu Thr Ala 450 455 460 Pro Pro Phe Leu Pro Glu Glu Leu Ala Val Val Gly Leu Asp Ala Ala 465 470 475 480 Thr Ile Ser Pro Thr Pro Thr Pro Thr Pro Thr Ala Ala Val Arg Ser 485 490 495 27 140 PRT Streptomyces cinnamonensis 27 Met Pro Asp Glu Ala Ala Arg Lys Gln Met Ala Val Asp Tyr Ala Glu 1 5 10 15 Arg Ile Asn Ala Gly Asp Ile Glu Gly Val Leu Asp Leu Phe Thr Asp 20 25 30 Asp Ile Val Phe Glu Asp Pro Val Gly Arg Pro Pro Met Val Gly Lys 35 40 45 Asp Asp Leu Arg Arg His Leu Glu Leu Ala Val Ser Cys Gly Thr His 50 55 60 Glu Val Pro Asp Pro Pro Met Thr Ser Met Asp Asp Arg Phe Val Val 65 70 75 80 Thr Pro Thr Thr Val Thr Val Gln Arg Pro Arg Pro Met Thr Phe Arg 85 90 95 Ile Val Gly Ile Val Glu Leu Asp Glu His Gly Leu Gly Arg Arg Val 100 105 110 Gln Ala Phe Trp Gly Val Thr Asp Val Thr Met Asp Asp Pro Ala Gly 115 120 125 Pro Ala Asp Thr Thr His Pro Glu Gly Ile Arg Ala 130 135 140 28 144 PRT Streptomyces cinnamonensis 28 Met Asn Glu Phe Ala Arg Lys Lys Arg Ala Leu Glu His Ser Arg Arg 1 5 10 15 Ile Asn Ala Gly Asp Leu Asp Ala Ile Ile Asp Leu Tyr Ala Pro Asp 20 25 30 Ala Val Leu Glu Asp Pro Val Gly Leu Pro Pro Val Thr Gly His Asp 35 40 45 Ala Leu Arg Ala His Tyr Glu Pro Leu Leu Ala Ala His Leu Arg Glu 50 55 60 Glu Ala Ala Glu Pro Val Ala Gly Gln Asp Ala Thr His Ala Leu Ile 65 70 75 80 Gln Ile Ser Ser Val Met Asp Tyr Leu Pro Val Gly Pro Leu Tyr Ala 85 90 95 Glu Arg Gly Trp Leu Lys Ala Pro Asp Ala Pro Gly Thr Ala Arg Ile 100 105 110 His Arg Thr Ala Met Leu Val Ile Arg Met Asp Ala Ser Gly Leu Ile 115 120 125 Arg His Leu Lys Ser Tyr Trp Gly Thr Ser Asp Leu Thr Val Leu Gly 130 135 140 29 3753 PRT Streptomyces cinnamonensis 29 Met Ser Asn Glu Glu Lys Leu Leu Asp His Leu Lys Trp Val Thr Ala 1 5 10 15 Glu Leu Arg Gln Ala Arg Gln Arg Leu His Asp Lys Glu Ser Thr Glu 20 25 30 Pro Val Ala Ile Val Gly Met Ala Cys Arg Tyr Pro Gly Gly Ala Arg 35 40 45 Ser Ala Glu Asp Leu Trp Glu Leu Val Arg Asp Gly Gly Asp Ala Val 50 55 60 Ala Gly Phe Pro Asp Asp Arg Gly Trp Asp Leu Glu Ser Leu Tyr His 65 70 75 80 Pro Asp Pro Glu His Pro Ala Thr Ser Tyr Val Arg Asp Gly Ala Phe 85 90 95 Leu Tyr Asp Ala Gly His Phe Asp Ala Glu Phe Phe Gly Ile Ser Pro 100 105 110 Arg Glu Ala Thr Ala Met Asp Pro Gln Gln Arg Leu Leu Leu Glu Thr 115 120 125 Ala Trp Glu Ala Ile Glu His Ala Gly Met Asn Pro His Ala Leu Lys 130 135 140 Gly Ser Asp Thr Gly Val Phe Thr Gly Val Ser Ala His Asp Tyr Leu 145 150 155 160 Thr Leu Ile Ser Gln Thr Ala Ser Asp Val Glu Gly Tyr Ile Gly Thr 165 170 175 Gly Asn Leu Gly Ser Val Val Ser Gly Arg Ile Ser Tyr Thr Val Gly 180 185 190 Leu Glu Gly Pro Ala Val Thr Val Asp Thr Ala Cys Ser Ser Ser Leu 195 200 205 Val Ala Ile His Leu Ala Ser Gln Ala Leu Arg Gln Gly Glu Cys Ser 210 215 220 Leu Ala Leu Ala Gly Gly Ser Thr Val Met Ala Thr Pro Gly Ser Phe 225 230 235 240 Thr Glu Phe Ser Arg Gln Arg Gly Leu Ala Pro Asp Gly Arg Cys Lys 245 250 255 Pro Phe Ala Ala Ala Ala Asp Gly Thr Gly Trp Gly Glu Gly Ala Gly 260 265 270 Val Val Ala Leu Glu Leu Leu Ser Glu Ala Arg Arg Arg Gly His Lys 275 280 285 Val Leu Ala Val Ile Arg Gly Ser Ala Thr Asn Gln Asp Gly Thr Ser 290 295 300 Asn Gly Leu Ala Ala Pro Asn Gly Pro Ser Gln Glu Arg Val Ile Arg 305 310 315 320 Ala Ala Leu Ala Asn Ala Arg Leu Ser Ala Glu Asp Ile Asp Ala Val 325 330 335 Glu Ala His Gly Thr Gly Thr Thr Leu Gly Asp Pro Ile Glu Ala Gln 340 345 350 Ala Leu Ile Ala Thr Tyr Gly Gln Gly Arg Pro Glu Asp Arg Pro Leu 355 360 365 Trp Leu Gly Ser Val Lys Ser Asn Ile Gly His Thr Gln Ala Ala Ala 370 375 380 Gly Val Ala Gly Val Ile Lys Met Val Met Ala Met Arg Asn Gly Leu 385 390 395 400 Leu Pro Thr Ser Leu His Ile Asp Ala Pro Ser Pro His Val Gln Trp 405 410 415 Glu Gln Gly Ser Val Arg Leu Leu Ser Glu Pro Val Asp Trp Pro Ala 420 425 430 Glu Arg Thr Arg Arg Ala Gly Ile Ser Ala Phe Gly Ile Ser Gly Thr 435 440 445 Asn Ala His Leu Ile Leu Glu Glu Ala Pro Pro Glu Glu Asp Ala Pro 450 455 460 Gly Pro Val Ala Ala Glu Pro Gly Gly Val Val Pro Trp Val Val Ser 465 470 475 480 Gly Arg Thr Pro Asp Ala Leu Arg Glu Gln Ala Arg Arg Leu Gly Glu 485 490 495 Phe Ala Ala Gly Leu Ala Asp Ala Ser Val Ser Glu Val Gly Trp Ser 500 505 510 Leu Ala Thr Thr Arg Ala Leu Phe Asp Gln Arg Ala Val Val Val Gly 515 520 525 Arg Asp Leu Ala Gln Ala Gly Ala Ser Leu Glu Ala Leu Ala Ala Gly 530 535 540 Glu Ala Ser Ala Asp Val Val Ala Gly Val Ala Gly Asp Val Gly Pro 545 550 555 560 Gly Pro Val Leu Val Phe Pro Gly Gln Gly Ser Gln Trp Val Gly Met 565 570 575 Gly Ala Gln Leu Leu Asp Glu Ser Pro Val Phe Ala Ala Arg Ile Ala 580 585 590 Glu Cys Glu Gln Ala Leu Ser Ala His Val Asp Trp Ser Leu Ser Asp 595 600 605 Val Leu Arg Gly Asp Gly Ser Glu Leu Ser Arg Val Glu Val Val Gln 610 615 620 Pro Val Leu Trp Ala Val Met Val Ser Leu Ala Ala Val Trp Ala Asp 625 630 635 640 Tyr Gly Ile Thr Pro Ala Ala Val Ile Gly His Ser Gln Gly Glu Met 645 650 655 Ala Ala Ala Cys Val Ala Gly Ala Leu Ser Leu Glu Asp Ala Ala Arg 660 665 670 Ile Val Ala Val Arg Ser Asp Ala Leu Arg Gln Leu Gln Gly His Gly 675 680 685 Asp Met Ala Ser Leu Ser Thr Gly Ala Glu Gln Ala Ala Glu Leu Ile 690 695 700 Gly Asp Arg Pro Gly Val Val Val Ala Ala Val Asn Gly Pro Ser Ser 705 710 715 720 Thr Val Ile Ser Gly Pro Pro Glu His Val Ala Ala Val Val Ala Asp 725 730 735 Ala Glu Ala Gln Gly Leu Arg Ala Arg Val Ile Asp Val Arg Tyr Ala 740 745 750 Ser His Gly Pro Gln Ile Asp Gln Leu His Asp Leu Leu Thr Asp Arg 755 760 765 Leu Ala Asp Ile Gln Pro Thr Thr Thr Asp Val Ala Phe Tyr Ser Thr 770 775 780 Val Thr Ala Glu Arg Leu Asp Asp Thr Thr Ala Leu Asp Thr Ala Tyr 785 790 795 800 Trp Val Thr Asn Leu Arg Gln Pro Val Arg Phe Ala Asp Thr Ile Glu 805 810 815 Ala Leu Leu Ala Asp Gly Tyr Arg Leu Phe Ile Glu Ala Ser Pro His 820 825 830 Pro Val Leu Asn Leu Gly Ile Gln Glu Thr Ile Glu Gln Gln Ala Gly 835 840 845 Ala Ala Gly Thr Ala Val Thr Ile Pro Thr Leu Arg Arg Asp His Gly 850 855 860 Asp Thr Thr Gln Leu Thr Arg Ala Ala Ala His Ala Phe Thr Ala Gly 865 870 875 880 Ala Pro Val Asp Trp Arg Arg Trp Phe Pro Ala Asp Pro Thr Pro Arg 885 890 895 Thr Val Asp Leu Pro Thr Tyr Ala Phe Gln His Lys His Tyr Trp Val 900 905 910 Glu Pro Pro Ala Ala Val Ala Ala Val Gly Gly Gly His Asp Pro Val 915 920 925 Glu Ala Arg Val Trp Gln Ala Ile Glu Asp Leu Asp Ile Asp Ala Leu 930 935 940 Ala Gly Ser Leu Glu Ile Glu Gly Gln Ala Glu Ser Val Gly Ala Leu 945 950 955 960 Glu Ser Ala Leu Pro Val Leu Ser Ala Trp Arg Arg Arg His Arg Glu 965 970 975 Gln Ser Thr Val Asp Ser Trp Arg Tyr Gln Val Thr Trp Lys His Leu 980 985 990 Pro Asp Val Pro Ala Pro Glu Leu Ser Gly Ala Trp Leu Leu Leu Val 995 1000 1005 Pro Ala Ala His Ala Asp His Pro Ala Val Leu Ala Thr Ala Gln Thr 1010 1015 1020 Leu Thr Ala His Gly Gly Glu Val Arg Arg His Val Val Asp Ala Arg 1025 1030 1035 1040 Ala Met Glu Arg Thr Glu Leu Ala Gln Glu Leu Arg Val Leu Met Asp 1045 1050 1055 Gly Ala Ala Phe Ala Gly Val Val Asn Leu Leu Ala Leu Asp Glu Glu 1060 1065 1070 Pro His Pro Glu His Ser Ala Val Pro Ala Gly Leu Ala Ala Thr Thr 1075 1080 1085 Ala Leu Val Gln Ala Leu Ala Asp Asn Gly Ala Asp Ile Ala Val Arg 1090 1095 1100 Thr Leu Thr Gln Gly Ala Val Ser Thr Ser Ala Gly Asp Ala Leu Thr 1105 1110 1115 1120 His Pro Val Gln Ala Gln Val Trp Gly Leu Gly Arg Val Ala Ala Leu 1125 1130 1135 Glu Tyr Pro Arg Leu Trp Gly Gly Leu Val Asp Leu Pro Ala Arg Ile 1140 1145 1150 Asp His Gln Thr Leu Ala Arg Leu Ala Ala Ala Leu Val Pro Gln Asp 1155 1160 1165 Glu Asp Gln Ile Ser Ile Arg Pro Ser Gly Val His Ala Arg Arg Leu 1170 1175 1180 Ala His Ala Pro Ala Asn Thr Val Gly Ser Gly Leu Gly Trp Arg Pro 1185 1190 1195 1200 Asp Gly Thr Thr Leu Ile Thr Gly Gly Thr Gly Gly Ile Gly Ala Val 1205 1210 1215 Leu Ala Arg Trp Leu Ala Arg Ala Gly Ala Pro His Leu Leu Leu Thr 1220 1225 1230 Ser Arg Arg Gly Pro Asp Ala Pro Gly Ala Gln Glu Leu Ala Ala Glu 1235 1240 1245 Leu Thr Glu Leu Gly Ala Ala Val Thr Val Thr Ala Cys Asp Val Gly 1250 1255 1260 Asp Arg Glu Gln Val Arg Arg Leu Ile Asp Asp Val Pro Ala Glu His 1265 1270 1275 1280 Pro Leu Thr Ala Val Ile His Ala Ala Gly Val Pro Asn Tyr Ile Gly 1285 1290 1295 Leu Gly Asp Val Ser Gly Ala Glu Leu Asp Glu Val Leu Arg Pro Lys 1300 1305 1310 Ala Leu Ala Ala His His Leu His Glu Leu Thr Arg Glu Leu Pro Leu 1315 1320 1325 Ser Ala Phe Val Met Phe Ser Ser Gly Ala Gly Val Trp Gly Ser Gly 1330 1335 1340 Gln Gln Gly Ala Tyr Gly Ala Ala Asn His Phe Leu Asp Ala Leu Ala 1345 1350 1355 1360 Glu His Arg Arg Ala Glu Gly Leu Pro Ala Thr Ser Ile Ala Trp Gly 1365 1370 1375 Pro Trp Ala Glu Ala Gly Met Ala Ala Asp Gln Ala Ala Leu Thr Phe 1380 1385 1390 Phe Ser Arg Phe Gly Leu His Pro Leu Ser Pro Glu Leu Cys Val Lys 1395 1400 1405 Ala Leu Gln Gln Ala Leu Asp Ala Gly Glu Thr Thr Leu Thr Val Ala 1410 1415 1420 Asn Phe Asp Trp Ala Gln Phe Thr Ser Thr Phe Thr Ala Gln Arg Pro 1425 1430 1435 1440 Ser Pro Leu Leu Ala Asp Leu Pro Glu Asn Arg Arg Ala Ser Ala Pro 1445 1450 1455 Ala Ala Gln Gln Glu Asp Ala Thr Glu Ala Ser Ser Leu Gln Gln Glu 1460 1465 1470 Leu Thr Glu Ala Lys Pro Ala Gln Gln Arg Gln Leu Leu Leu Gln His 1475 1480 1485 Val Arg Ser Gln Ala Ala Ala Thr Leu Gly His Ser Asp Val Asp Ala 1490 1495 1500 Val Pro Ala Thr Lys Pro Phe Gln Glu Leu Gly Phe Asp Ser Leu Thr 1505 1510 1515 1520 Ala Val Glu Leu Arg Asn Arg Leu Asn Lys Ser Thr Gly Leu Thr Leu 1525 1530 1535 Pro Thr Thr Val Val Phe Asp His Pro Thr Pro Asp Ala Leu Thr Asp 1540 1545 1550 Val Leu Arg Ala Glu Leu Ser Gly Asp Ala Ala Ala Ser Ala Asp Pro 1555 1560 1565 Val Arg Ala Ala Gly Ala Ser Arg Gly Ala Ala Asp Asp Glu Pro Ile 1570 1575 1580 Ala Ile Val Gly Met Ala Cys Arg Tyr Pro Gly Asp Val Arg Ser Ala 1585 1590 1595 1600 Glu Glu Leu Trp Asp Leu Val Ala Ala Gly Lys Asp Ala Met Gly Ala 1605 1610 1615 Phe Pro Asp Asp Arg Gly Trp Asp Leu Glu Thr Leu Tyr Asp Pro Asp 1620 1625 1630 Pro Glu Ser Arg Gly Thr Ser Tyr Val Arg Glu Gly Gly Phe Leu Tyr 1635 1640 1645 Asp Ala Gly Asp Phe Asp Ala Gly Phe Phe Gly Ile Ser Pro Arg Glu 1650 1655 1660 Ala Val Ala Met Asp Pro Gln Gln Arg Leu Leu Leu Glu Thr Ala Trp 1665 1670 1675 1680 Glu Ala Ile Glu Arg Ala Gly Leu Asp Arg Glu Thr Leu Lys Gly Ser 1685 1690 1695 Asp Ala Gly Val Phe Thr Gly Leu Thr Ile Phe Asp Tyr Leu Ala Leu 1700 1705 1710 Val Gly Glu Gln Pro Thr Glu Val Glu Gly Tyr Ile Gly Thr Gly Asn 1715 1720 1725 Leu Gly Cys Val Ala Ser Gly Arg Val Ser Tyr Val Leu Gly Leu Glu 1730 1735 1740 Gly Pro Ala Met Thr Ile Asp Thr Gly Cys Ser Ser Ser Leu Val Ala 1745 1750 1755 1760 Ile His Gln Ala Ala His Ala Leu Arg Gln Gly Glu Cys Ser Leu Ala 1765 1770 1775 Leu Ala Gly Gly Ala Thr Val Met Ala Thr Pro Gly Ser Phe Val Glu 1780 1785 1790 Phe Ser Leu Gln Arg Gly Leu Ala Lys Asp Gly Arg Cys Lys Pro Phe 1795 1800 1805 Ala Ala Ala Ala Asp Gly Thr Gly Trp Ala Glu Gly Val Gly Leu Val 1810 1815 1820 Val Leu Glu Arg Leu Ser Glu Ala Arg Arg Asn Gly His Asn Val Leu 1825 1830 1835 1840 Ala Val Ile Arg Gly Ser Ala Ile Asn Gln Asp Gly Thr Ser Asn Gly 1845 1850 1855 Leu Thr Ala Pro Asn Gly Gln Ala Gln Gln Arg Val Ile Arg Gln Ala 1860 1865 1870 Leu Ala Asn Ala Arg Leu Ser Ala Glu Asp Val Asp Ala Val Glu Ala 1875 1880 1885 His Gly Thr Gly Thr Met Leu Gly Asp Pro Ile Glu Ala Ser Ala Leu 1890 1895 1900 Val Ala Thr Tyr Gly Lys Glu Arg Pro Ala Asp Arg Pro Leu Trp Leu 1905 1910 1915 1920 Gly Ser Ile Lys Ser Asn Ile Gly His Ala Gln Ala Ser Ala Gly Val 1925 1930 1935 Ala Gly Val Ile Lys Met Val Met Ala Leu Arg Asn Glu Gln Leu Pro 1940 1945 1950 Ala Ser Leu His Ile Asp Ala Pro Thr Pro His Val Asp Trp Asp Gly 1955 1960 1965 Ser Gly Val Arg Leu Leu Ser Glu Pro Val Ser Trp Pro Arg Gly Glu 1970 1975 1980 Arg Pro Arg Arg Ala Gly Val Ser Ala Phe Gly Ile Ser Gly Thr Asn 1985 1990 1995 2000 Ala His Leu Ile Leu Glu Gln Ala Pro Asp Ala Pro Glu Pro Val Thr 2005 2010 2015 Ala Pro Ala Glu Asp Ala Ala Ala Pro Ala Gly Val Val Pro Trp Val 2020 2025 2030 Val Ser Ala Arg Gly Glu Glu Ala Leu Arg Ala Gln Ala Arg Leu Leu 2035 2040 2045 Ala Asp Arg Ala Thr Ala Asp Pro Arg Leu Ala Ser Pro Leu Asp Val 2050 2055 2060 Gly Trp Ser Leu Val Lys Thr Arg Ser Val Phe Glu Asn Arg Ala Val 2065 2070 2075 2080 Val Val Gly Lys Asp Arg Gln Thr Leu Leu Ala Gly Leu Arg Ser Leu 2085 2090 2095 Ala Ala Gly Glu Pro Ser Pro Asp Val Val Glu Gly Ala Val Gln Gly 2100 2105 2110 Ala Ser Gly Ala Gly Pro Val Leu Val Phe Pro Gly Gln Gly Ser Gln 2115 2120 2125 Trp Val Gly Met Gly Ala Gln Leu Leu Asp Glu Ser Pro Val Phe Ala 2130 2135 2140 Ala Arg Ile Ala Glu Cys Glu Arg Ala Leu Ser Ala His Val Asp Trp 2145 2150 2155 2160 Ser Leu Ser Ala Val Leu Arg Gly Asp Gly Ser Glu Leu Ser Arg Val 2165 2170 2175 Glu Val Val Gln Pro Val Leu Trp Ala Val Met Val Ser Leu Ala Ser 2180 2185 2190 Val Trp Ala Asp Tyr Gly Ile Thr Pro Ala Ala Val Ile Gly His Ser 2195 2200 2205 Gln Gly Glu Met Ala Ala Ala Cys Val Ala Gly Ala Leu Ser Leu Glu 2210 2215 2220 Asp Ala Ala Arg Ile Val Ala Val Arg Ser Asp Ala Leu Arg Gln Leu 2225 2230 2235 2240 Met Gly Gln Gly Asp Met Ala Ser Leu Gly Ala Gly Ser Glu Gln Val 2245 2250 2255 Ala Glu Leu Ile Gly Asp Arg Pro Gly Val Cys Val Ala Ala Val Asn 2260 2265 2270 Gly Pro Ser Ser Thr Val Ile Ser Gly Pro Pro Glu His Val Ala Ala 2275 2280 2285 Val Val Ala Asp Ala Glu Ala Arg Gly Leu Arg Ala Arg Val Ile Asp 2290 2295 2300 Val Gly Tyr Ala Ser His Gly Pro Gln Ile Asp Gln Leu His Asp Leu 2305 2310 2315 2320 Leu Thr Glu Arg Leu Ala Asp Ile Arg Pro Thr Thr Thr Asp Val Ala 2325 2330 2335 Phe Tyr Ser Thr Val Thr Ala Glu Arg Leu Asp Asp Thr Thr Thr Leu 2340 2345 2350 Asp Thr Asp Tyr Trp Val Thr Asn Leu Arg Gln Pro Val Arg Phe Ala 2355 2360 2365 Asp Thr Ile Glu Ala Leu Leu Ala Asp Gly Tyr Arg Leu Phe Ile Glu 2370 2375 2380 Ala Ser Pro His Pro Val Leu Asn Leu Gly Met Glu Glu Thr Ile Glu 2385 2390 2395 2400 Arg Ala Asp Met Pro Ala Thr Val Val Pro Thr Leu Arg Arg Asp His 2405 2410 2415 Gly Asp Ala Ala Gln Leu Thr Arg Ala Ala Ala Gln Ala Phe Gly Ala 2420 2425 2430 Gly Ala Glu Val Asp Trp Thr Gly Trp Phe Pro Ala Val Pro Leu Pro 2435 2440 2445 Arg Val Val Asp Leu Pro Thr Tyr Ala Phe Gln Arg Glu Arg Phe Trp 2450 2455 2460 Leu Glu Gly Arg Arg Gly Leu Ala Gly Asp Pro Ala Gly Leu Gly Leu 2465 2470 2475 2480 Ala Ser Ala Gly His Pro Leu Leu Gly Ala Ala Val Glu Leu Ala Asp 2485 2490 2495 Gly Gly Ser His Leu Leu Thr Gly Arg Ile Ser Pro Arg Asp Gln Ala 2500 2505 2510 Trp Leu Ala Glu His Arg Val Met Asp Thr Val Leu Leu Pro Gly Ser 2515 2520 2525 Ala Phe Val Glu Leu Ala Leu Gln Ala Ala Val Arg Ala Gly Cys Ala 2530 2535 2540 Glu Leu Ala Glu Leu Thr Leu His Thr Pro Leu Ala Phe Gly Asp Glu 2545 2550 2555 2560 Gly Ala Gly Ala Val Asp Val Gln Val Val Val Gly Ser Val Ala Glu 2565 2570 2575 Asp Gly Arg Arg Pro Val Thr Val His Ser Arg Pro Thr Gly Glu Gly 2580 2585 2590 Glu Glu Ala Val Trp Thr Arg His Ala Ala Gly Val Val Ala Pro Pro 2595 2600 2605 Gly Pro Asp Ala Gly Asp Ala Ser Phe Gly Gly Thr Trp Pro Pro Pro 2610 2615 2620 Gly Ala Thr Pro Val Gly Glu Gln Asp Pro Tyr Gly Glu Leu Ala Ser 2625 2630 2635 2640 Tyr Gly Tyr Asp Phe Gly Pro Gly Ser Gln Gly Leu Val Ser Ala Trp 2645 2650 2655 Arg Leu Gly Asp Asp Leu Phe Ala Glu Val Ala Leu Pro Glu Ala Glu 2660 2665 2670 Ser Gly Arg Ala Asp Arg Tyr Gln Val His Pro Val Leu Leu Asp Ala 2675 2680 2685 Thr Leu His Ala Leu Ile Leu Asp Ala Val Thr Ser Ser Ala Asp Thr 2690 2695 2700 Asp Gln Val Leu Leu Pro Phe Ser Trp Ser Gly Leu Arg Val His Ala 2705 2710 2715 2720 Pro Gly Ala Glu Lys Leu Arg Val Arg Ile Ala Arg Thr Ala Pro Asp 2725 2730 2735 Gln Leu Ala Leu Thr Ala Val Asp Gly Gly Gly Gly Gly Glu Pro Val 2740 2745 2750 Leu Thr Leu Glu Ser Leu Thr Val Arg Pro Val Ala Ala His Gln Ile 2755 2760 2765 Ala Gly Ala Arg Ala Ala Asp Arg Asp Ala Leu Phe Arg Leu Val Trp 2770 2775 2780 Met Glu Val Ala Ala Arg Ala Glu Glu Thr Gly Gly Gly Ala Pro Arg 2785 2790 2795 2800 Ala Ala Val Leu Ala Pro Val Glu Ser Gly Pro Met Gly Gly Thr Ser 2805 2810 2815 Ala Gly Ala Leu Ala Asp Ala Leu Ser Asp Ala Leu Ala Ala Gly Pro 2820 2825 2830 Val Trp Asp Thr Phe Gly Ala Leu Arg Asp Gly Val Ala Ala Gly Gly 2835 2840 2845 Glu Ala Pro Asp Val Val Leu Ala Val Cys Ala Ala Pro Gly Ala Gly 2850 2855 2860 Ala Gly Ala Val Ala Asp Ala Asp Gly Arg Gly Gly Asp Pro Ala Gly 2865 2870 2875 2880 Tyr Ala Arg Leu Ala Thr Val Ser Leu Leu Ser Leu Leu Lys Glu Trp 2885 2890 2895 Val Asp Asp Pro Ala Phe Ala Ala Thr Arg Leu Val Val Val Thr Arg 2900 2905 2910 Gly Ala Val Ala Ala Arg Pro Gly Glu Thr Ala Gly Asp Leu Ala Gly 2915 2920 2925 Ala Ser Leu Trp Gly Leu Val Arg Ser Ala Gln Ala Glu Asn Pro Gly 2930 2935 2940 Arg Leu Thr Leu Leu Asp Val Asp Gly Leu Glu Ser Ser Pro Ala Thr 2945 2950 2955 2960 Leu Thr Gly Val Leu Ala Ser Gly Glu Pro Glu Leu Ala Leu Arg Asp 2965 2970 2975 Gly Arg Ala Tyr Val Pro Arg Leu Val Arg Asp Asp Ala Ser Val Arg 2980 2985 2990 Leu Val Pro Pro Val Gly Ser Leu Thr Trp Arg Leu Ala Arg Cys Gln 2995 3000 3005 Glu Ala Gly Gly Gly Gln Gln Leu Ser Leu Val Asp Ala Pro Glu Ala 3010 3015 3020 Gly Arg Ala Leu Glu Pro His Glu Val Arg Val Ala Val Arg Ala Ala 3025 3030 3035 3040 Ala Pro Gly Pro Leu Thr Ala Gly Gln Val Glu Gly Ala Gly Val Val 3045 3050 3055 Thr Glu Val Gly Gly Glu Val Gly Ser Val Ala Val Gly Asp Arg Val 3060 3065 3070 Met Gly Leu Phe Asp Ala Val Gly Pro Val Ala Val Thr Asp Ala Ala 3075 3080 3085 Leu Leu Met Pro Val Pro Ala Gly Trp Ser Trp Ala Gln Ala Ala Gly 3090 3095 3100 Ser Leu Gly Ala Tyr Val Ser Ala Tyr His Val Leu Ala Asp Val Val 3105 3110 3115 3120 Ala Pro Arg Gly Gly Glu Thr Leu Leu Val Gly Glu Glu Thr Gly Ser 3125 3130 3135 Val Gly Arg Ala Val Leu Arg Leu Ala Leu Ala Gly Arg Trp Arg Val 3140 3145 3150 Glu Ala Val Asp Gly Ala Ser Thr Ala Asp Asp Ser Gly Ala Glu Arg 3155 3160 3165 Ala Ala Asp Val Thr Leu Arg His Glu Gly Ala Leu Val Val His Arg 3170 3175 3180 Ala Gly Gly Arg Pro Asp Glu Gly Gln Ala Val Val Pro Pro Glu Pro 3185 3190 3195 3200 Gly Arg Val Arg Glu Ile Leu Ala Glu Leu Thr Glu Leu Thr Glu Leu 3205 3210 3215 Ala Glu Ile Thr Glu Ser Ala Glu Pro Gly Leu Pro Ala Glu Arg Gly 3220 3225 3230 Asp Ser Arg Ala Leu Thr Pro Leu Asp Ile Thr Val Trp Asp Ile Arg 3235 3240 3245 Gln Ala Pro Ala Ala Met Ala Ala Pro Pro Ser Ala Gly Thr Thr Val 3250 3255 3260 Phe Ser Leu Pro Pro Ala Phe Asp Pro Glu Gly Thr Val Leu Val Thr 3265 3270 3275 3280 Gly Gly Thr Gly Ala Leu Gly Ser Leu Thr Ala Arg His Leu Val Glu 3285 3290 3295 Arg Tyr Gly Ala Arg His Leu Leu Leu Ser Ser Arg Arg Gly Ala Asp 3300 3305 3310 Ala Pro Gly Ala Leu Glu Leu Ala Ala Asp Leu Ser Ala Leu Gly Ala 3315 3320 3325 Arg Val Thr Phe Ala Ala Cys Asp Pro Gly Asp Arg Asp Glu Ala Ala 3330 3335 3340 Ala Leu Leu Ala Ala Val Pro Ser Asp His Pro Leu Thr Ala Val Phe 3345 3350 3355 3360 His Cys Ala Gly Thr Val Asn Asp Ala Val Val Gln Asn Leu Thr Ala 3365 3370 3375 Glu Gln Val Glu Glu Val Met Arg Val Lys Ala Asp Ala Ala Trp His 3380 3385 3390 Leu His Glu Leu Thr Arg Asp Ala Asp Leu Ser Ala Phe Val Leu Tyr 3395 3400 3405 Ser Ser Val Ala Gly Leu Leu Gly Gly Pro Gly Gln Gly Ser Tyr Thr 3410 3415 3420 Ala Ala Asn Ala Phe Leu Asp Ala Leu Ala Arg His Arg His Asp Gly 3425 3430 3435 3440 Gly Ala Ala Ala Thr Ser Leu Ala Trp Gly Tyr Trp Glu Leu Ala Ser 3445 3450 3455 Gly Met Ser Gly Arg Leu Thr Asp Ala Asp Arg Ala Arg His Ala Arg 3460 3465 3470 Ala Gly Val Val Gly Leu Gly Ala Asp Glu Gly Leu Ala Leu Leu Asp 3475 3480 3485 Ala Ala Trp Ala Gly Gly Leu Pro Leu Tyr Ala Pro Val Arg Leu Asp 3490 3495 3500 Leu Ala Arg Met Arg Arg Gln Ala Gln Ser His Pro Ala Pro Ala Leu 3505 3510 3515 3520 Leu Arg Asp Leu Val Arg Gly Gly Ser Lys Ser Gly Gly Gly Ala Val 3525 3530 3535 Ser Ala Gly Ala Ala Ala Leu Leu Lys Ser Leu Gly Ala Met Ser Asp 3540 3545 3550 Pro Glu Arg Glu Glu Ala Leu Leu Asp Leu Val Cys Thr His Ile Ala 3555 3560 3565 Ala Val Leu Gly Tyr Asp Ala Ala Thr Pro Val Asn Ala Thr Gln Gly 3570 3575 3580 Leu Arg Glu Leu Gly Phe Asp Ser Leu Thr Ala Val Glu Leu Arg Asn 3585 3590 3595 3600 Arg Leu Ser Ala Ala Thr Gly Leu Lys Leu Pro Ala Thr Phe Val Phe 3605 3610 3615 Asp His Pro Asn Pro Ala Glu Leu Ala Ala Gln Leu Arg Gln Glu Leu 3620 3625 3630 Ala Pro Arg Ala Ala Asp Pro Leu Ala Asp Val Leu Ala Glu Phe Glu 3635 3640 3645 Arg Ile Glu Asp Ser Leu Leu Ser Val Ser Ser Lys Asp Gly Ser Ala 3650 3655 3660 Arg Ala Glu Leu Ala Gly Arg Leu Arg Ala Thr Leu Ala Arg Leu Asp 3665 3670 3675 3680 Ala Pro Gln Asp Thr Ala Gly Glu Val Ala Val Ala Thr Arg Thr Arg 3685 3690 3695 Ile Gln Asp Ala Ser Ala Asp Glu Ile Phe Ala Phe Ile Asp Arg Asp 3700 3705 3710 Leu Gly Arg Asp Gly Ala Ser Gly Gln Gly Asn Gly Gln Pro Thr Gly 3715 3720 3725 Gln Gly Asn Gly His Gly Asn Gly Asn Gly Asn Gly Asn Gly Asn Gly 3730 3735 3740 His Gly Gln Ala Val Glu Gly Gln Arg 3745 3750 30 1641 PRT Streptomyces cinnamonensis 30 Met Ala His Thr Glu Glu Lys Leu Leu Glu Tyr Leu Lys Arg Val Thr 1 5 10 15 Ala Asp Leu Arg Gln Thr Glu Arg Arg Leu Gln Asp Val Glu Ser Ala 20 25 30 Gly His Glu Pro Val Ala Val Ile Gly Met Ala Cys Arg Leu Pro Gly 35 40 45 Gly Val Arg Ser Pro Glu Glu Phe Trp Glu Leu Val Ser Thr Gly Gly 50 55 60 Asp Ala Val Ala Pro Leu Pro Gly Asn Arg Asn Trp Asp Leu Asp Ser 65 70 75 80 Leu Tyr Asp Pro Asp Pro Glu Ser Thr Gly Thr Ser Tyr Val Arg Glu 85 90 95 Gly Gly Phe Val Tyr Asp Ala Gly Asp Phe Asp Pro Thr Phe Phe Gly 100 105 110 Ile Gly Pro Thr Glu Ala Ala Ala Met Ala Pro Gln Gln Arg Leu Ala 115 120 125 Leu Glu Thr Ala Trp Glu Ala Ile Glu Arg Ala Gly Ile Asp Pro Leu 130 135 140 Ser Leu Arg Ser Ser Asp Thr Ser Thr Phe Ile Gly Cys Asp Gly Leu 145 150 155 160 Asp Tyr Ala Leu Gly Ala Ser Glu Val Pro Glu Gly Thr Ala Gly Tyr 165 170 175 Phe Thr Ile Gly Asn Ser Gly Ser Val Thr Ser Gly Arg Val Ala Tyr 180 185 190 Thr Leu Gly Leu Glu Gly Pro Ala Val Thr Val Asp Thr Ala Cys Ser 195 200 205 Ser Ser Leu Val Ser Leu His Leu Ala Thr Gln Ala Leu Arg Thr Gln 210 215 220 Glu Cys Ser Leu Ala Leu Ala Gly Gly Thr Tyr Val Met Ser Ser Pro 225 230 235 240 Ala Pro Leu Ile Gly Phe Ser Glu Leu Arg Gly Leu Ala Pro Asp Gly 245 250 255 Arg Cys Lys Pro Phe Ser Ala Ser Ser Asp Gly Met Gly Met Ala Glu 260 265 270 Gly Thr Gly Val Val Leu Leu Glu Arg Leu Ser Asp Ala Arg Arg Lys 275 280 285 Gly His Lys Val Leu Ala Val Ile Arg Gly Ser Ala Ile Asn Gln Asp 290 295 300 Gly Ala Ser Asn Gly Leu Thr Ala Pro Asn Gly Pro Ala Gln Glu Arg 305 310 315 320 Val Ile Arg Ala Ala Leu Ala Asn Ala Arg Leu Ala Pro Glu Asp Ile 325 330 335 Asp Ala Val Glu Ala His Gly Thr Gly Thr Thr Leu Gly Asp Pro Ile 340 345 350 Glu Ala Gly Ala Leu Ile Ser Ala Tyr Gly Arg Glu Arg Pro Glu Asp 355 360 365 Arg Pro Leu Trp Val Gly Ala Val Lys Ser Asn Ile Gly His Thr Gln 370 375 380 Ile Ala Ala Gly Val Ala Gly Val Ile Lys Met Val Leu Ala Leu Arg 385 390 395 400 His Asp Leu Leu Pro Ala Ile Leu His Val Asp Ala Pro Ser Pro His 405 410 415 Val Glu Trp Asp Gly Ser Gly Leu Arg Leu Leu Thr Asp Pro Val Lys 420 425 430 Trp Pro Arg Gly Glu Arg Pro Arg Arg Ala Gly Val Ser Ser Phe Gly 435 440 445 Phe Ser Gly Thr Asn Ala His Leu Ile Leu Glu Glu Ala Pro Pro Glu 450 455 460 Glu Glu Asp Val Pro Gly Ser Val Ala Glu Glu Pro Gly Gly Val Val 465 470 475 480 Pro Trp Val Val Ser Gly Arg Thr Pro Asp Ala Leu Arg Ala Gln Ala 485 490 495 Arg Arg Leu Gly Glu Phe Ala Ala Gly Pro Ala Asp Ala Ser Ala Ala 500 505 510 Asp Val Gly Trp Ser Leu Thr Thr Thr Arg Ser Val Phe Glu His Arg 515 520 525 Ala Val Val Val Gly Arg Asp Arg Asp Ala Leu Thr Ala Gly Leu Gly 530 535 540 Ala Leu Ala Ala Gly Glu Ala Ser Ala Gly Val Val Ala Gly Val Ala 545 550 555 560 Gly Asp Val Gly Pro Gly Pro Val Leu Val Phe Pro Gly Gln Gly Ser 565 570 575 Gln Trp Val Gly Met Gly Ala Gln Leu Leu Asp Glu Ser Pro Val Phe 580 585 590 Ala Ala Arg Ile Ala Glu Cys Glu Arg Ala Leu Ser Ala Tyr Val Asp 595 600 605 Trp Ser Leu Ser Ala Val Leu Arg Gly Asp Gly Ser Glu Leu Ser Arg 610 615 620 Val Glu Val Val Gln Pro Val Leu Trp Ala Val Met Val Ser Leu Ala 625 630 635 640 Ala Val Trp Ala Asp Tyr Gly Val Thr Pro Ala Ala Val Ile Gly His 645 650 655 Ser Gln Gly Glu Met Ala Ala Ala Cys Val Ala Gly Ala Leu Ser Leu 660 665 670 Glu Asp Ala Ala Arg Ile Val Ala Val Arg Ser Asp Ala Leu Arg Arg 675 680 685 Leu Gln Gly His Gly Asp Met Ala Ser Leu Ser Thr Gly Ala Glu Gln 690 695 700 Ala Ala Glu Leu Ile Gly Asp Arg Pro Gly Val Val Val Ala Ala Val 705 710 715 720 Asn Gly Pro Ser Ser Thr Val Ile Ser Gly Pro Pro Glu His Val Ala 725 730 735 Ala Val Val Ala Asp Ala Glu Ala Arg Gly Leu Arg Ala Arg Val Ile 740 745 750 Asp Val Gly Tyr Ala Ser His Gly Pro Gln Ile Asp Gln Leu His Asp 755 760 765 Leu Leu Thr Glu Arg Leu Ala Asp Ile Arg Pro Ala Asn Thr Asp Val 770 775 780 Ala Phe Tyr Ser Thr Val Thr Ala Glu Arg Leu Thr Asp Thr Thr Ala 785 790 795 800 Leu Asp Thr Asp Tyr Trp Val Thr Asn Leu Arg Gln Pro Val Arg Phe 805 810 815 Ala Asp Thr Ile Glu Ala Leu Leu Ala Asp Gly Tyr Arg Leu Phe Ile 820 825 830 Glu Ala Ser Ala His Pro Val Leu Gly Leu Gly Met Glu Glu Thr Ile 835 840 845 Glu Gln Ala Asp Ile Pro Ala Thr Val Val Pro Thr Leu Arg Arg Asp 850 855 860 His Gly Asp Thr Thr Gln Leu Thr Arg Ala Ala Ala His Ala Phe Thr 865 870 875 880 Ala Gly Ala Pro Val Asp Trp Arg Arg Trp Phe Pro Ala Asp Pro Thr 885 890 895 Pro Arg Thr Val Asp Leu Pro Thr Tyr Ala Phe Gln His Gln His Tyr 900 905 910 Trp Leu Glu Arg Ser Ala Ser Ala Ser Gly Ala Val Ser Gly Glu Gln 915 920 925 Ser Ala Ala Glu Ala Gln Leu Trp His Ala Val Glu Glu Leu Asp Leu 930 935 940 Gly Leu Leu Ala Glu Thr Leu Gly Ser Glu Glu Gly Ser Glu Glu Ala 945 950 955 960 Val Arg Ala Leu Glu Pro Ala Leu Pro Val Leu Lys Gly Trp Arg Arg 965 970 975 Arg His Gln Asp Gln Ala Thr Ile Asp Ser Trp Arg Tyr Arg Val Thr 980 985 990 Trp Lys Gln Arg Ser Asp Gly Pro Ala Pro Glu Leu Gly Gly Asp Trp 995 1000 1005 Leu Leu Phe Val Pro Ala Asp Lys Ala Glu His Pro Ala Val Arg Ala 1010 1015 1020 Thr Ala Glu Ala Leu Ser Glu His Gly Ala Ala Ala Val Arg Leu His 1025 1030 1035 1040 Pro Val Glu Thr Gly Arg Ala Gly Arg Gln Glu Leu Ala Ala Val Asp 1045 1050 1055 Thr Ala Gly Leu Ala Gly Ile Val Asn Leu Leu Ala Leu Asp Glu Glu 1060 1065 1070 Pro His Pro Glu His Pro Ala Val Pro Ala Gly Leu Ala Ala Thr Thr 1075 1080 1085 Ala Leu Leu Gln Ala Leu Gly Asp Asn Gly Thr Thr Ala Pro Leu His 1090 1095 1100 Thr Val Thr Gln Gly Ala Val Ser Thr Gly Ala Thr Asp Pro Leu Thr 1105 1110 1115 1120 His Pro Leu Gln Ala His Val Trp Gly Leu Gly Arg Val Ala Ala Leu 1125 1130 1135 Glu His Pro Arg Leu Trp Ala Gly Leu Val Asp Leu Pro Ala Arg Ile 1140 1145 1150 Asp Arg His Thr Leu Pro Arg Leu Ala Ala Ala Leu Leu Pro Gln Asp 1155 1160 1165 Asp Glu Asp Gln Thr Ala Val Arg Pro Thr Gly Ile His His Arg Arg 1170 1175 1180 Leu Thr His Ala Val Gly Ser Ile Gln Asn Pro Val His Ser Glu Ala 1185 1190 1195 1200 Thr Trp Arg Pro Arg Gly Thr Thr Leu Ile Thr Gly Gly Thr Gly Gly 1205 1210 1215 Ile Gly Ala Val Leu Ala Arg Trp Leu Ala Arg Gln Gly Ala Pro Arg 1220 1225 1230 Leu His Leu Thr Ser Arg Arg Gly Pro Asp Ala Pro Gly Ala Arg Glu 1235 1240 1245 Leu Ala Ala Glu Leu Asp Gly Leu Gly Thr Ala Val Thr Ile Thr Ala 1250 1255 1260 Cys Asp Val Ser Asp Pro Arg Gln Leu Ser Gly Leu Ile Asp Asp Met 1265 1270 1275 1280 Pro Ala Glu His Pro Leu Thr Ala Val Ile His Ala Ala Gly Met Thr 1285 1290 1295 Asp Leu Thr Ala Ile Gly Asp Leu Thr Thr Ala Arg Leu Gly Glu Val 1300 1305 1310 Leu Gly Ser Lys Ser Asp Ala Ala Trp Asn Leu His Glu Leu Thr Arg 1315 1320 1325 Asp Leu Asp Leu Ser Ala Phe Val Met Phe Ser Ser Gly Ala Gly Val 1330 1335 1340 Trp Gly Ser Gly Gln Gln Gly Ala Tyr Gly Ala Ala Asn His Phe Leu 1345 1350 1355 1360 Asp Ala Leu Ala Glu His Arg Arg Ala Gln Gly Leu Pro Ala Thr Ser 1365 1370 1375 Ile Ala Trp Gly Pro Trp Ala Glu Ala Gly Met Ser Ala Asp Pro Glu 1380 1385 1390 Ser Leu Thr Tyr Phe Lys Arg Phe Gly Leu Leu Pro Ile Ala Pro Asp 1395 1400 1405 Leu Cys Val Lys Ala Leu His Gln Ala Val Asp Ala Gly Asp Ala Thr 1410 1415 1420 Leu Thr Val Ala Asn Phe Asp Trp Ala Lys Phe Thr Pro Thr Phe Thr 1425 1430 1435 1440 Ala Gln Arg Pro Ser Pro Phe Leu Asp Asp Leu Pro Glu Asn Gln Arg 1445 1450 1455 Glu Ala Glu Gln Thr Gly Thr Ala Ala Glu Thr Ser Ala Phe Arg Glu 1460 1465 1470 Glu Leu Ala Lys Thr Pro Ala Ser Gln Arg Leu Gly Phe Leu Val Gln 1475 1480 1485 Gln Val Arg Thr Tyr Ala Ala Ala Thr Leu Gly Arg Thr Val Glu Asp 1490 1495 1500 Ile Pro Ala Ala Lys Pro Phe Gln Glu Leu Gly Phe Asp Ser Leu Thr 1505 1510 1515 1520 Ala Val Gln Leu Arg Asn Gln Leu Asn Thr Thr Thr Gly Leu Ser Leu 1525 1530 1535 Pro Ala Thr Val Ile Phe Asp His Pro Thr Pro Glu Ala Leu Ala Thr 1540 1545 1550 His Leu Arg Gly Gln Leu Gly Asp Gly Ala Glu Val Ala Gly Glu Gly 1555 1560 1565 Asp Val Leu Ala Ala Leu Asp Lys Trp Asp Thr Ala Phe Gly Ala Ala 1570 1575 1580 Glu Val Asp Glu Ala Ala Arg Arg Arg Ile Val Gly Arg Leu Gln Val 1585 1590 1595 1600 Leu Val Ser Lys Trp Ser Pro Ala Gln Asp Gly Pro Glu Gly Thr Asp 1605 1610 1615 Ser Ala His Ala Asp Leu Glu Ala Ala Ser Ala Asp Asp Ile Phe Asp 1620 1625 1630 Leu Ile Ser Ser Glu Phe Gly Lys Ser 1635 1640 31 430 PRT Streptomyces cinnamonensis 31 Val Gly Leu Thr Val Gly Pro Asp Asn Ala Lys Arg Gly Ile Val Pro 1 5 10 15 Ile Thr Asp Ser Lys Pro Ala Ala Thr Phe Pro Asp Leu Val Asp Pro 20 25 30 Ser Phe Trp Ala Arg Pro His Ala Glu Arg Val Ala Leu Phe Glu Glu 35 40 45 Met Arg Gly Leu Pro Arg Pro Ala Phe Ile Arg Gln Asn Met Pro Gly 50 55 60 Val Pro Trp Thr Phe Gly Tyr His Ala Leu Val Lys Tyr Ala Asp Ile 65 70 75 80 Val Glu Val Ser Arg Arg Pro Gln Asp Phe Ser Ser Asn Gly Ala Thr 85 90 95 Thr Ile Ile Gly Leu Pro Pro Glu Leu Asp Glu Tyr Tyr Gly Ser Met 100 105 110 Ile Asn Met Asp Asn Pro Glu His Ser Arg Leu Arg Arg Ile Val Ser 115 120 125 Arg Ser Phe Gly Arg Asn Met Ile Pro Glu Phe Glu Ala Val Ala Thr 130 135 140 Arg Thr Ala Arg Arg Ile Ile Asp Glu Leu Ile Ala Arg Gly Pro Gly 145 150 155 160 Asp Phe Ile Arg Pro Val Ala Ala Glu Met Pro Ile Ala Val Leu Ser 165 170 175 Asp Met Met Gly Ile Pro Ala Glu Asp His Asp Phe Leu Phe Asp Arg 180 185 190 Ser Asn Thr Ile Val Gly Pro Leu Asp Pro Asp Tyr Val Pro Asp Arg 195 200 205 Ala Asp Ser Glu Arg Ala Val Ile Glu Ala Ser Arg Glu Leu Gly Asp 210 215 220 Tyr Ile Ala Gly Leu Arg Ala Glu Arg Leu Ala Ala Pro Gly Asn Asp 225 230 235 240 Leu Ile Thr Lys Leu Val Gln Val Gln Ala Asp Gly Glu Gln Leu Thr 245 250 255 Arg Gln Glu Leu Val Ser Phe Phe Ile Leu Leu Val Ile Ala Gly Met 260 265 270 Glu Thr Thr Arg Asn Ala Ile Ser His Ala Leu Val Leu Leu Thr Glu 275 280 285 His Pro Glu Gln Lys Gln Leu Leu Leu Ser Asp Phe Asp Thr His Ala 290 295 300 Pro Asn Ala Val Glu Glu Ile Leu Arg Val Ser Thr Pro Ile Asn Trp 305 310 315 320 Met Arg Arg Val Ala Thr Arg Asp Cys Asp Met Asn Gly His Arg Phe 325 330 335 Arg Arg Gly Asp Arg Ile Phe Leu Phe Tyr Trp Ser Gly Asn Arg Asp 340 345 350 Glu Ser Val Phe Pro Asp Pro Tyr Arg Phe Asp Ile Thr Arg Gly Thr 355 360 365 Asn Ala His Val Thr Phe Gly Ala Val Gly Pro His Val Cys Leu Gly 370 375 380 Ala His Leu Ala Arg Met Glu Ile Thr Val Leu Tyr Arg Glu Leu Leu 385 390 395 400 Ala Ala Leu Pro Gln Ile His Ala Val Gly Gln Pro Arg Arg Leu Asp 405 410 415 Ser Ser Phe Ile Glu Gly Ile Lys His Leu His Cys Ala Phe 420 425 430 32 267 PRT Streptomyces cinnamonensis 32 Val Arg Tyr Glu Met Leu Gly Pro Leu Arg Ile Lys Asp Gly Asn Asp 1 5 10 15 Tyr Ala Thr Ile Asn Ala Gln Lys Val Glu Ile Val Leu Thr Val Leu 20 25 30 Leu Ile Arg Ala Asp Arg Val Val Ser Leu Glu Gln Leu Met Arg Glu 35 40 45 Ile Trp Gly Glu Asp Leu Pro Arg Arg Ala Thr Ala Gly Leu His Val 50 55 60 Tyr Ile Ser Gln Leu Arg Lys Phe Leu Lys Val Pro Gly Ser Ala Gly 65 70 75 80 Asn Pro Val Glu Thr Arg Ala Pro Gly Tyr Val Leu His Lys Arg Asp 85 90 95 Asp Asp Gln Ile Asp Ala Gln Ile Phe Pro Glu Leu Val Asp Val Gly 100 105 110 Arg Ser Leu Leu Arg Glu Lys Arg Phe Asp Glu Ala Ala Ser Cys Phe 115 120 125 Gly Gln Ala Leu Ala Leu Trp Arg Gly Pro Ile Leu Gly Gln Gly Gly 130 135 140 Asn Gly Pro Gly Thr Asn Gly Pro Ile Ile Asp Gly Phe Ser Thr Trp 145 150 155 160 Leu Thr Glu Ile Arg Leu Glu Cys Gln Glu Met Leu Val Glu Cys Gln 165 170 175 Leu Gln Leu Gly Arg His Arg Glu Ala Val Gly Met Leu Tyr Ala Leu 180 185 190 Thr Ala Glu Asn Pro Met Cys Glu Ala Phe Tyr Arg Gln Leu Met Leu 195 200 205 Ala Leu Tyr Arg Ser Glu Arg Gln Ala Asp Ala Leu Lys Val Tyr Gln 210 215 220 Ser Val Arg Lys Thr Leu Asn Asp Glu Leu Gly Leu Glu Pro Gly Arg 225 230 235 240 Pro Leu Gln Glu Leu Gln Arg Ala Ile Leu Ala Gly Asp Met His Leu 245 250 255 Met Ser Pro Pro Pro Leu Ala Leu Ser Gly Arg 260 265 33 277 PRT Streptomyces cinnamonensis 33 Leu Ser Ala Phe Leu Ala Lys Gly Lys Ile Leu Ser Ala Phe Pro Pro 1 5 10 15 Pro Asp Met Ser Asp Pro Trp Ile Arg Arg Phe Arg Pro Arg Pro Glu 20 25 30 Ala Val Val Arg Leu Val Cys Phe Pro His Ala Gly Gly Ser Ala Ser 35 40 45 Tyr Tyr His Pro Leu Ala Gln Ser Pro Thr Leu Pro Thr Asp Ser Glu 50 55 60 Val Leu Ala Val Gln Tyr Pro Gly Arg Gln Asp Arg Arg Arg Glu Arg 65 70 75 80 Leu Leu Asp Asp Ile Gly Glu Leu Ala Asp Leu Ile Thr Asp Ala Leu 85 90 95 Gly Pro Phe Asp Asp Arg Pro Leu Ala Phe Phe Gly His Ser Met Gly 100 105 110 Ala Val Leu Ala Tyr Glu Val Ala Gln Arg Leu Arg Glu Arg Thr Gly 115 120 125 Lys Gln Pro Cys Arg Leu Phe Val Ser Gly Arg Arg Ala Pro Ser Arg 130 135 140 Phe Arg Arg Gly Thr Val His Leu Leu Asp Asp Thr Glu Leu Ala Ala 145 150 155 160 Glu Leu Arg Arg Ala Gly Gly Thr Asp Pro Arg Phe Leu Asp Asp Glu 165 170 175 Glu Leu Leu Ala Glu Ile Ile Pro Val Val Arg Asn Asp Tyr Arg Ala 180 185 190 Val Glu Leu Tyr Arg Trp Asn Pro Ser Pro Pro Leu Ser Cys Pro Ile 195 200 205 Thr Ala Leu Val Gly Asp Arg Asp Pro Gln Ala Pro Leu Asp Glu Val 210 215 220 Glu Ala Trp Gln Gln His Thr Glu Gly Pro Phe Asp Leu Lys Val Phe 225 230 235 240 Ala Gly Gly His Phe Tyr Leu Asn Thr His Gln Gln Gly Val Thr Glu 245 250 255 Val Ile Ser Lys Ala Leu Ala Asp Ser Ala Gln Gln Arg Ala Thr Ala 260 265 270 Arg Gly Asn Ala Arg 275 34 427 PRT Streptomyces cinnamonensis 34 Leu Ala Asp Leu Val Ala His Ala Arg Ser Ala Ser Pro Tyr Tyr Arg 1 5 10 15 Glu Leu Tyr His Gly Leu Pro Glu Arg Ile Glu Asp Pro Thr Leu Leu 20 25 30 Pro Val Thr Asp Lys Lys Gln Leu Met Asp His Phe Asp Asp Trp Pro 35 40 45 Thr Asp Arg Asp Ile Thr Phe Glu Lys Val Arg Ala Phe Thr Asp Asp 50 55 60 Pro Glu Leu Ile Gly Arg Arg Phe Leu Gly Arg Tyr Leu Val Ala Thr 65 70 75 80 Thr Ser Gly Thr Ser Gly Arg Arg Gly Leu Phe Val Leu Asp Asp Arg 85 90 95 Tyr Met Asn Val Ser Ser Ala Val Ser Ser Arg Val Leu Ala Ser Trp 100 105 110 Leu Gly Pro Leu Gly Ile Ala Arg Ala Val Val His Gly Gly Arg Phe 115 120 125 Ala Gln Leu Val Ala Thr Glu Gly His Tyr Val Gly Phe Ala Gly Tyr 130 135 140 Ser Arg Leu Arg Gln Asp Gly Glu Ala Arg Ser Lys Leu Val Arg Ala 145 150 155 160 Phe Ser Val His Glu Pro Met Ser Arg Leu Val Ala Glu Leu Asn Glu 165 170 175 Tyr Arg Pro Ala Phe Val Ile Gly Tyr Ala Ser Thr Ile Met Leu Phe 180 185 190 Thr Ala Glu Gln Glu Ala Gly Arg Leu His Ile Asp Pro Val Leu Val 195 200 205 Glu Pro Ala Gly Glu Thr Met Thr Glu Ser Asp Thr Asp Arg Ile Ala 210 215 220 Ala Ala Phe Gly Ala Lys Val Arg Thr Met Tyr Ser Ala Thr Glu Cys 225 230 235 240 Thr Tyr Leu Ser His Gly Cys Ala Glu Gly Trp Tyr His Val Asn Asp 245 250 255 Asp Trp Ala Val Leu Glu Pro Val Asp Ala Asp His Arg Pro Thr Pro 260 265 270 Pro Gly Glu Phe Ser His Thr Thr Leu Ile Ser Asn Leu Ala Asn Arg 275 280 285 Val Gln Pro Phe Leu Arg Tyr Asp Leu Gly Asp Ser Val Met Leu Arg 290 295 300 Pro Asp Pro Cys Pro Cys Gly Thr Pro Ser Pro Ala Ile Arg Val Gln 305 310 315 320 Gly Arg Ser Gly Asp Ile Leu Thr Phe Pro Ser Gly Arg Gly Asp Asp 325 330 335 Val Ser Leu Ala Pro Leu Ala Phe Ser Ser Leu Phe Asp Arg Met Pro 340 345 350 Gly Val Glu Leu Phe Gln Ile Glu Gln Thr Ala Pro Ser Thr Leu Arg 355 360 365 Val Arg Val Val Gln Ala Pro Gly Ala Asp Ala Asp His Val Trp Gln 370 375 380 Arg Ala His Asp Gly Leu Thr His Leu Leu Ala Asp Asn Lys Leu Asp 385 390 395 400 Asn Val Thr Val Glu Arg Gly Glu Glu Pro Pro Arg Gln Ala Ser Gly 405 410 415 Gly Lys Tyr Arg Thr Ile Ile Pro Leu Ala Ala 420 425 35 338 PRT Streptomyces cinnamonensis 35 Val Lys Val Pro Val Glu Val Thr Val Arg Leu Ser Ser Trp Leu Gly 1 5 10 15 Gly Leu Val Ala Ala Val Leu Ala Ala Thr Val Leu Pro Ala Ser Ala 20 25 30 Ala Ser Ala Ala Asp Val Ser Ser Pro Pro Leu Glu Ile Pro Ala Ala 35 40 45 Glu Leu Ala Lys Ala Leu His Cys Gly Thr Glu Leu Gly Asp Leu Arg 50 55 60 Asp Ala Gly Asp Lys Pro Thr Val Leu Phe Val Pro Gly Thr Gly Leu 65 70 75 80 Lys Gly Glu Glu Asn Tyr Ala Trp Asn Tyr Met Ala Glu Leu Lys Lys 85 90 95 Lys Gly Tyr Gln Ser Cys Trp Val Asp Ser Pro Gly Arg Gly Leu Arg 100 105 110 Asp Met Gln Glu Ser Val Glu Tyr Val Val Tyr Ala Thr Arg Ala Ile 115 120 125 Gln Glu Ala Thr Gly Arg Lys Val Asp Leu Val Gly His Ser Gln Gly 130 135 140 Gly Leu Leu Thr Ala Trp Ala Leu Arg Phe Trp Pro Asp Leu Pro Gly 145 150 155 160 Lys Val Asp Asp Met Val Thr Leu Gly Ser Pro Phe Gln Gly Thr Arg 165 170 175 Leu Ala Ser Pro Cys Arg Pro Ile Ala Glu Val Ala Gly Cys Pro Ala 180 185 190 Ser Val Leu Gln Phe Ala Arg Asp Ser Asn Trp Ser Lys Ala Leu Gly 195 200 205 Ala Asp Gly Thr Pro Met Pro Ala Gly Pro Ser Tyr Thr Thr Ile Tyr 210 215 220 Ser Tyr Ala Asp Glu Ser Val Val Ala Asp Gly Glu Ala Pro Ser Leu 225 230 235 240 Pro Gly Ala His Arg Ile Gly Val Gln Asp Ile Cys Pro Gly Arg Pro 245 250 255 Trp Pro Thr His Ile Ala Met Val Val Asp Gln Val Ser Tyr Asp Leu 260 265 270 Val Ala Asp Ala Ile Glu His Pro Gly Pro Ala Asp Thr Ser Arg Ile 275 280 285 Asp Arg Ala His Cys Ala Lys Pro Val Met Pro Leu Asn Ser Gln Glu 290 295 300 Ala Val Asp Ala Leu Pro Gly Leu Leu Asn Phe Pro Ile Glu Leu Leu 305 310 315 320 Ile His Ser Gln Pro Trp Val Asp Glu Glu Pro Pro Leu Arg Pro Tyr 325 330 335 Ala Arg 36 308 PRT Streptomyces cinnamonensis 36 Met Gly His Asp His Gly Pro Ser Ala Gly Ala Ala Gly Gly Thr Leu 1 5 10 15 Ser Gly Thr Tyr Arg Lys Arg Leu Leu Trp Thr Ile Gly Ile Ser Gly 20 25 30 Ser Ile Thr Val Ile Gln Val Val Gly Ala Leu Leu Ser Gly Ser Leu 35 40 45 Ala Leu Leu Ala Asp Ala Ala His Ser Leu Thr Asp Ala Val Gly Val 50 55 60 Ser Leu Ala Leu Gly Ala Ile Thr Leu Ala Gln Arg Ala Pro Thr Pro 65 70 75 80 Arg Arg Thr Phe Gly Phe Cys Arg Val Glu Ile Phe Ser Ala Val Leu 85 90 95 Asn Ala Leu Leu Leu Val Val Ile Phe Ala Trp Val Leu Trp Ser Ala 100 105 110 Ile Gly Arg Phe Ser Glu Pro Val Glu Val Lys Gly Gly Leu Met Phe 115 120 125 Val Val Ala Leu Gly Gly Leu Ala Ala Asn Leu Val Gly Leu Trp Leu 130 135 140 Leu Arg Asp Ala Lys Glu Lys Ser Leu Asn Leu Arg Gly Ala Tyr Leu 145 150 155 160 Glu Val Leu Gly Asp Ala Leu Gly Ser Val Ala Val Ile Val Gly Gly 165 170 175 Leu Val Ile Leu Leu Thr Gly Trp Gln Ala Ala Asp Pro Ile Ala Ser 180 185 190 Ile Val Ile Gly Leu Leu Ile Val Pro Arg Ala Tyr Gly Leu Leu Arg 195 200 205 Asp Ser Leu His Val Leu Leu Glu Ala Thr Pro Gln Asp Val Asp Leu 210 215 220 Gly Glu Val Arg Arg His Leu Leu Glu Glu Arg Gly Val Val Ala Val 225 230 235 240 His Asp Leu His Gly Trp Thr Val Thr Ser Gly Met Pro Val Leu Thr 245 250 255 Ala His Val Val Val Thr Glu Glu Ala Leu Ala Ser Gly Tyr Gly Glu 260 265 270 Leu Leu Gly Arg Leu Gln Arg Cys Val Gly Gly His Phe Asp Val Ala 275 280 285 His Ser Thr Ile Gln Leu Glu Pro Glu Gly His Val Glu Glu Asp Gly 290 295 300 Ala Leu His Thr 305 37 363 PRT Streptomyces cinnamonensis 37 Met Thr Arg Ala Leu Thr Leu His Asp Trp Ile Val Ala Gly Ile Ala 1 5 10 15 Val Val Ala Gly Val Val Ala Gly Leu Leu Leu Arg Ala Leu Leu Arg 20 25 30 Trp Leu Gly Glu Arg Ala Ser Lys Thr Arg Trp Ser Gly Asp Asp Val 35 40 45 Ile Val Asp Ala Leu Arg Thr Leu Val Pro Cys Ala Ala Ile Thr Ala 50 55 60 Gly Leu Ala Ala Ala Ala Gly Ala Leu Pro Leu Thr Pro Arg Thr Gly 65 70 75 80 Arg Asn Val Thr Met Thr Leu Thr Ala Leu Leu Ile Leu Ala Ala Thr 85 90 95 Leu Thr Ala Ala Arg Ile Val Thr Gly Leu Val Lys Ala Val Ala Gln 100 105 110 Ser Arg Ser Gly Val Ala Gly Ser Ala Thr Ile Phe Val Asn Ile Thr 115 120 125 Arg Val Val Val Leu Ala Met Gly Phe Leu Ile Val Leu Gln Thr Leu 130 135 140 Gly Ile Ser Ile Ala Pro Leu Leu Thr Ala Leu Gly Val Gly Gly Leu 145 150 155 160 Ala Val Ala Leu Ala Leu Gln Asp Thr Leu Ala Asn Leu Phe Ala Gly 165 170 175 Val His Ile Leu Ala Ala Lys Thr Val Gln Pro Gly Asp Tyr Ile Gln 180 185 190 Leu Ser Ser Gly Glu Glu Gly Tyr Val Val Asp Ile Asn Trp Arg Asn 195 200 205 Thr Thr Val Arg Gln Leu Ser Asn Asn Leu Val Ile Ile Pro Asn Ala 210 215 220 Lys Leu Ala Gly Thr Asn Met Thr Asn Tyr Ser Arg Pro Glu Gln Glu 225 230 235 240 Leu Ser Ile Met Val Gln Val Gly Val Ser Tyr Asp Ser Asp Leu Glu 245 250 255 Gln Val Glu Lys Val Thr Thr Glu Val Val Asp Glu Val Met Ala Glu 260 265 270 Ile Thr Gly Ala Val Pro Asp His Glu Ala Ala Ile Arg Phe His Thr 275 280 285 Phe Gly Asp Ser Arg Ile Ser Phe Thr Val Ile Leu Gly Val Gly Glu 290 295 300 Phe Ser Asp Gln Tyr Arg Ile Lys His Glu Phe Ile Lys Arg Leu His 305 310 315 320 Gln Arg Tyr Arg Ala Glu Gly Ile Arg Val Pro Ala Pro Val Arg Thr 325 330 335 Val Arg Val Gln Gln Gly Glu Leu Pro Pro Pro Leu Gly Ile Pro His 340 345 350 Gln Arg Asp Thr Ser Thr Gln Ala Arg Leu His 355 360 38 131 PRT Streptomyces cinnamonensis 38 Met Ser Pro Val Asn Ser His Asn Glu Trp Asp Pro Leu Glu Glu Ile 1 5 10 15 Ile Val Gly Arg Leu Glu Gly Ala Thr Ile Pro Ser Ser His Pro Val 20 25 30 Val Ala Cys Asn Ile Pro Thr Trp Ala Ala Arg Leu Gln Gly Leu Ala 35 40 45 Ala Gly Phe Glu Tyr Pro Gln Arg Leu Ile Glu Pro Ala Gln Gln Glu 50 55 60 Leu Asp Gln Phe Ile Ala Leu Leu Gln Ser Leu Asp Val Thr Val Arg 65 70 75 80 Arg Pro Ala Ala Val Asp His Lys His Arg Phe Gly Thr Pro Asp Trp 85 90 95 Gln Ser Arg Gly Phe Cys Asn Ser Cys Pro Arg Asp Ser Met Leu Val 100 105 110 Val Gly Asp Glu Ile Ile Glu Thr Pro Met Ala Trp Pro Cys Arg Cys 115 120 125 Phe Glu Thr 130 39 32 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide 39 ccactagtat gcatgcgagt gtccgttcga gt 32 40 29 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide 40 ttgtatacac ctaggatggt tggccgtgc 29 41 29 DNA Artificial Sequence Description of Artificial Sequence Primer 41 agataccata tgctgggccc gctccgcat 29 42 35 DNA Artificial Sequence Description of Artificial Sequence Primer 42 aatgctctag actgtcagcg accggacagg gccaa 35 43 35 DNA Artificial Sequence Description of Artificial Sequence Primer 43 ggtggccacg gaaacaccaa caccggaccc gcgcc 35 44 29 DNA Artificial Sequence Description of Artificial Sequence Primer 44 ctctcggagg cccggcgcaa cggccacaa 29 45 34 DNA Artificial Sequence Description of Artificial Sequence Primer 45 ggcctagggc tgcctcgggt ggtggatctg ccga 34 46 27 DNA Artificial Sequence Description of Artificial Sequence Primer 46 tggtcgggcg cggtgcgtgc gatacgt 27 47 30 DNA Artificial Sequence Description of Artificial Sequence Primer 47 cctggccagg gcggccagtg ggtgggcatg 30 48 35 DNA Artificial Sequence Description of Artificial Sequence Primer 48 ggcctagggg tcggccggga accagcgccg ccagt 35 49 31 DNA Artificial Sequence Description of Artificial Sequence Primer 49 gtgacgtcat atgtcgagtg ctgaagagtc g 31 50 32 DNA Artificial Sequence Description of Artificial Sequence Primer 50 ggggtcgcct aggaaccagc gccgccagtc ga 32 51 50 DNA Artificial Sequence Description of Artificial Sequence Primer 51 cggcctcgag ggcccgtcgg tcagtgtcga cacggcgcag tcctcctcgc 50 52 32 DNA Artificial Sequence Description of Artificial Sequence Primer 52 ggggtcgcct aggaaccagc gccgccagtc ga 32 

1. A DNA sequence which is (a) at least part of the sequence set out in the appended sequence listing; or (b) a variant of a sequence (a) which encodes a polypeptide which is at least 80%, preferably at least 90%, identical with the corresponding peptide as set out in table II; provided that it is not a sequence encoding all or part of the polypeptide consisting of amino acids 1-920 encoded by mon AI as set out in table II.
 2. A DNA sequence according to claim 1 comprising the complete monensin gene cluster or a variant thereof.
 3. A DNA sequence encoding at least part of at least one polypeptide which is necessary for the biosynthesis of monensin, and which is encoded by DNA included in the appended sequence listing or an allele, mutation or other variant thereof; provided that said polypeptide is not all or part of amino acids 1-920 encoded by mon AI as set out in table II.
 4. A DNA sequence according to claim 3 which comprises at least part of one or more of the following genes: mon BI, mon BII, mon CI, mon CII, mon H, mon RI, mon RII, mon T, mon AIX and mon AX.
 5. A DNA sequence according to claim 4 comprising all of the genes listed therein or an allele, mutation or other variant thereof.
 6. A DNA sequence according to claim 3 encoding at least part of one or more of the polypeptides set out below, said polypeptide having the amino acid sequence as set out in the appended sequence data or being a variant thereof having the specified activity: peptide activity mon CII epoxyhydrolase/cyclase mon E S-adenosylmethionine-dependent methyltransferase mon T monensin resistance gene mon RII repressor protein mon AIX thioesterase mon AI polyketide synthase multienzyme mon AII polyketide synthase multienzyme mon AIII polyketide synthase multienzyme mon AIV polyketide synthase multienzyme mon AV polyketide synthase multienzyme mon AVI polyketide synthase multienzyme mon AVII polyketide synthase multienzyme mon AVIII polyketide synthase multienzyme mon H regulatory protein mon CI flavin-dependent epoxidase mon BII carbon—carbon double bond isomerase mon BI carbon—carbon double bond isomerase mon D cytochrome P450 hydroxylase mon RI activator protein mon AX thioesterase


7. A DNA sequence according to claim 6 encoding a single enzyme activity of a multienzyme encoded by any of mon AI-mon AVIII or a variant or part thereof.
 8. A DNA sequence according to any preceding claim encoding any one or more of the domains as set out in Table I or a variant or part thereof.
 9. A DNA sequence according to any preceding claim which has a length of at least 30, preferably at least 60, bases.
 10. A recombinant cloning or expression vector comprising a DNA sequence according to any preceding claim.
 11. A transformant host cell which has been transformed to contain a DNA sequence according to any of claims 1-9 and which is capable of expressing a corresponding polypeptide.
 12. A hybridisation probe which is a DNA sequence according to any of claims 1-9.
 13. Use of a probe according to claim 12 to detect a PKS cluster, optionally followed by isolation of the detected cluster.
 14. Use of a probe according to claim 12 which encodes at least part of a polypeptide having a known function to detect genes encoding polypeptides having analogous function.
 15. Use according to claim 14 wherein the polypeptide of known function is AT of module 5 or the regulatory protein encoded by mon RI.
 16. A hybridization probe comprising a polynucleotide which binds specifically to a region of the monensin gene cluster selected from mon BI, mon BII, mon CI, mon CII, mon H, mon RI, mon RII, mon T, mon AIX and mon AX.
 17. Use of a probe according to claim 16 in a method of detecting the presence of a gene cluster which governs the synthesis of a polyether, and optionally isolating a gene cluster detected thereby.
 18. Use of a probe according to claim 12 which comprise a polynucleotide which binds specifically to a gene responsible for levels of activity of the monensin gene cluster, in a method of detecting an analogous gene in a gene cluster for biosynthesis of another polyketide, optionally followed by a step of manipulating the gene detected thereby to alter the level of expression of said other polyketide.
 19. Use according to claim 18 wherein the gene is a regulatory gene, resistance gene or thioesterase gene.
 20. Use of the mon RI gene or variant and a monensin promoter to control expression of a heterologous gene in S. cinnamonensis.
 21. Use of a portion of the monensin gene cluster encoding a polypeptide having chain terminating activity, preferably comprising at least one of mon AIX and mon AX or a mutant, allele or other variant thereof encoding a polypeptide having chain terminating activity, to effect chain release of a peptide other than monensin.
 22. Use of a portion of the monensin gene cluster encoding a polypeptide having carbon-carbon double bond isomerase activity, preferably comprising at least one of mon BI and mon BII or a mutant, allele or other variant thereof having isomerase activity to provide a desired stereochemical outcome in the synthesis of a polyketide other than monensin.
 23. A polypeptide encoded by a portion of the monensin gene cluster, preferably comprising at least one of mon BI and mon BII or a mutant, allele or other variant thereof, having carbon-carbon double bond isomerase activity, or at least one of mon AIX and mon AX or a mutant, allele or other variant thereof having chain terminating activity.
 24. An epoxidase enzyme encoded by mon CI or a derivative or variant thereof having epoxidase activity.
 25. A cyclase enzyme encoded by mon CII or a derivative or variant thereof having cyclase activity.
 26. Use of a portion of the monensin gene cluster encoding a peptide having epoxidase or cyclase activity, preferably comprising mon CI or mon CII or a mutant, allele or other variant thereof encoding a polypeptide having epoxidase or cyclase activity to provide a said activity in the biosynthesis of a polypeptide other than monensin.
 27. A process for producing a polyketide containing a desired starter unit comprising providing a PKS gene having a loading module and a plurality of extension modules, wherein the loading module includes a KS_(q) domain derived from a KS domain of a monensin extension module.
 28. A process according to claim 27 wherein the KS_(q) domain is derived from KS of module 5 of monensin.
 29. A process according to claim 27 or claim 28 wherein the starter unit also includes an AT_(q) domain derived from an AT domain which is naturally associated with the KS domain.
 30. A DNA sequence comprising DNA encoding at least one PKS loading module and a plurality of PKS extension modules, and which can be expressed to produce a polyketide; wherein at least one of said modules or at least one domain thereof is a monensin module or domain or a variant thereof and is contiguous to a further one of said modules or a domain to which it is not naturally contiguous; provided that the sequence is not an ery loading module, the first and second extension modules of the ery PKS and the ery chain-terminating thioesterase in which the DNA encoding AT of the first extension module has been substituted by DNA encoding an ethyl malonyl-CoA AT from the monensin gene cluster.
 31. A DNA sequence according to claim 30 wherein said further module or domain is also a monensin module or domain or variant thereof.
 32. A DNA sequence according to claim 30 wherein said further module or domain is a module or domain of a PKS of a polyketide other than monensin or a variant thereof.
 33. A DNA sequence according to claim 30, 31 or 32 wherein said loading module is adapted to load a starter unit other than a starter unit normally received by the adjacent extension module.
 34. A DNA sequence according to claim 33 wherein said loading module is derived from a monensin extension module or variant thereof.
 35. A polyketide synthase encoded by the DNA sequence of any of claims 30-34.
 36. A polyketide compound as produced by a synthase according to claim
 35. 37. A vector containing a DNA sequence of any of claims 30-34.
 38. A transformant cell transformed to contain a DNA sequence of any of claims 30-34.
 39. A method of producing S. cinnamonensis capable of enhanced levels of production of monensin comprising engineering it to overexpress the mon RI gene.
 40. A method according to claim 39 wherein said engineering comprises introducing at least one additional copy of the mon RI gene as shown in the appended sequence data or a variant thereof.
 41. S. cinnamonensis containing multiple copies of the mon RI gene as shown in the appended sequence data and/or variant(s) thereof.
 42. A method of producing monensin comprising culturing the organism of claim 41 and/or an organism produced by the method of claim 39 or claim
 40. 43. A process for expressing a gene heterologous to S. cinnamonensis comprising transforming S. cinnamonensis with DNA encoding a heterologous gene and expressing said gene under control of the activator gene mon RI or actII/orf4.
 44. A process according to claim 43 wherein said heterologous gene is a PKS gene.
 45. 13-Propyl erythromycin A. 